Crystal Structure of Scallop Myosin S1 in the Pre-Power Stroke State to 2.6 Å Resolution: Flexibility and Function in the Head
We have extended the X-ray structure determination of the complete scallop myosin head in the pre-power stroke state to 2.6 Å resolution, allowing an atomic comparison of the three major (weak actin binding) states of various myosins. We can now account for conformational differences observed in cry...
Gespeichert in:
| Veröffentlicht in: | Structure (London) 2003-12, Vol.11 (12), p.1621-1627 |
|---|---|
| Hauptverfasser: | , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 1627 |
|---|---|
| container_issue | 12 |
| container_start_page | 1621 |
| container_title | Structure (London) |
| container_volume | 11 |
| creator | Gourinath, S. Himmel, Daniel M. Brown, Jerry H. Reshetnikova, Ludmilla Szent-Györgyi, Andrew G. Cohen, Carolyn |
| description | We have extended the X-ray structure determination of the complete scallop myosin head in the pre-power stroke state to 2.6 Å resolution, allowing an atomic comparison of the three major (weak actin binding) states of various myosins. We can now account for conformational differences observed in crystal structures in the so-called “pliant region” at the motor domain-lever arm junction between scallop and vertebrate smooth muscle myosins. A hinge, which may contribute to the compliance of the myosin crossbridge, has also been identified for the first time within the regulatory light-chain domain of the lever arm. Analysis of temperature factors of key joints of the motor domain, especially the SH1 helix, provides crystallographic evidence for the existence of the “internally uncoupled” state in diverse isoforms. The agreement between structural and solution studies reinforces the view that the unwinding of the SH1 helix is a part of the cross-bridge cycle in many myosins. |
| doi_str_mv | 10.1016/j.str.2003.10.013 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_proquest_miscellaneous_71428504</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0969212603002569</els_id><sourcerecordid>71428504</sourcerecordid><originalsourceid>FETCH-LOGICAL-e191t-34546a3826e8f1d8f88443ce9db273f91c0d3ae5181478651ef30ea6384c96f53</originalsourceid><addsrcrecordid>eNo1kcFO3DAQhq2qCBbKA_SCfOotwRM7Xqc9oVUXKoGKuuVseZ2J6sUbL7ZT2BMnnqwv1kTAZX7NzKdfo_kJ-QysBAbyfFOmHMuKMT72JQP-gcxAzVUhQMmPZMYa2RQVVPKIHKe0YYxVNWOH5AiErKUQ9Yw8L-I-ZePpKsfB5iEiDR1dWeN92NGbfUiupyugY81_kN5GLG7DI8aJD_c4islIc6BVKem_F_oLU_BDdqH_Spcen9zaeZf31PQtXQ69nTbvZldo2k_koDM-4embnpC75fffi6vi-uflj8XFdYHQQC64qIU0XFUSVQet6pQSglts2nU1510DlrXcYA0KxFzJGrDjDI3kSthGdjU_IV9efXcxPAyYst66ZNF702MYkp6DqFTNxAievYHDeout3kW3NXGv3182At9eARzP_esw6mQd9hZbF9Fm3QangekpIL3RY0B6CmgajQHx_67rgjk</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>71428504</pqid></control><display><type>article</type><title>Crystal Structure of Scallop Myosin S1 in the Pre-Power Stroke State to 2.6 Å Resolution: Flexibility and Function in the Head</title><source>MEDLINE</source><source>Cell Press Free Archives</source><source>Elsevier ScienceDirect Journals</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>Free Full-Text Journals in Chemistry</source><creator>Gourinath, S. ; Himmel, Daniel M. ; Brown, Jerry H. ; Reshetnikova, Ludmilla ; Szent-Györgyi, Andrew G. ; Cohen, Carolyn</creator><creatorcontrib>Gourinath, S. ; Himmel, Daniel M. ; Brown, Jerry H. ; Reshetnikova, Ludmilla ; Szent-Györgyi, Andrew G. ; Cohen, Carolyn</creatorcontrib><description>We have extended the X-ray structure determination of the complete scallop myosin head in the pre-power stroke state to 2.6 Å resolution, allowing an atomic comparison of the three major (weak actin binding) states of various myosins. We can now account for conformational differences observed in crystal structures in the so-called “pliant region” at the motor domain-lever arm junction between scallop and vertebrate smooth muscle myosins. A hinge, which may contribute to the compliance of the myosin crossbridge, has also been identified for the first time within the regulatory light-chain domain of the lever arm. Analysis of temperature factors of key joints of the motor domain, especially the SH1 helix, provides crystallographic evidence for the existence of the “internally uncoupled” state in diverse isoforms. The agreement between structural and solution studies reinforces the view that the unwinding of the SH1 helix is a part of the cross-bridge cycle in many myosins.</description><identifier>ISSN: 0969-2126</identifier><identifier>EISSN: 1878-4186</identifier><identifier>DOI: 10.1016/j.str.2003.10.013</identifier><identifier>PMID: 14656445</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Actins - chemistry ; Animals ; Crystallography, X-Ray ; Electrons ; Models, Molecular ; Mollusca ; Muscle, Smooth - metabolism ; Myosin Subfragments - chemistry ; Myosins - chemistry ; Nucleic Acid Conformation ; Protein Binding ; Protein Conformation ; Protein Isoforms ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Temperature ; Vanadates - chemistry</subject><ispartof>Structure (London), 2003-12, Vol.11 (12), p.1621-1627</ispartof><rights>2003 Cell Press</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0969212603002569$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/14656445$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gourinath, S.</creatorcontrib><creatorcontrib>Himmel, Daniel M.</creatorcontrib><creatorcontrib>Brown, Jerry H.</creatorcontrib><creatorcontrib>Reshetnikova, Ludmilla</creatorcontrib><creatorcontrib>Szent-Györgyi, Andrew G.</creatorcontrib><creatorcontrib>Cohen, Carolyn</creatorcontrib><title>Crystal Structure of Scallop Myosin S1 in the Pre-Power Stroke State to 2.6 Å Resolution: Flexibility and Function in the Head</title><title>Structure (London)</title><addtitle>Structure</addtitle><description>We have extended the X-ray structure determination of the complete scallop myosin head in the pre-power stroke state to 2.6 Å resolution, allowing an atomic comparison of the three major (weak actin binding) states of various myosins. We can now account for conformational differences observed in crystal structures in the so-called “pliant region” at the motor domain-lever arm junction between scallop and vertebrate smooth muscle myosins. A hinge, which may contribute to the compliance of the myosin crossbridge, has also been identified for the first time within the regulatory light-chain domain of the lever arm. Analysis of temperature factors of key joints of the motor domain, especially the SH1 helix, provides crystallographic evidence for the existence of the “internally uncoupled” state in diverse isoforms. The agreement between structural and solution studies reinforces the view that the unwinding of the SH1 helix is a part of the cross-bridge cycle in many myosins.</description><subject>Actins - chemistry</subject><subject>Animals</subject><subject>Crystallography, X-Ray</subject><subject>Electrons</subject><subject>Models, Molecular</subject><subject>Mollusca</subject><subject>Muscle, Smooth - metabolism</subject><subject>Myosin Subfragments - chemistry</subject><subject>Myosins - chemistry</subject><subject>Nucleic Acid Conformation</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>Protein Isoforms</subject><subject>Protein Structure, Secondary</subject><subject>Protein Structure, Tertiary</subject><subject>Temperature</subject><subject>Vanadates - chemistry</subject><issn>0969-2126</issn><issn>1878-4186</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo1kcFO3DAQhq2qCBbKA_SCfOotwRM7Xqc9oVUXKoGKuuVseZ2J6sUbL7ZT2BMnnqwv1kTAZX7NzKdfo_kJ-QysBAbyfFOmHMuKMT72JQP-gcxAzVUhQMmPZMYa2RQVVPKIHKe0YYxVNWOH5AiErKUQ9Yw8L-I-ZePpKsfB5iEiDR1dWeN92NGbfUiupyugY81_kN5GLG7DI8aJD_c4islIc6BVKem_F_oLU_BDdqH_Spcen9zaeZf31PQtXQ69nTbvZldo2k_koDM-4embnpC75fffi6vi-uflj8XFdYHQQC64qIU0XFUSVQet6pQSglts2nU1510DlrXcYA0KxFzJGrDjDI3kSthGdjU_IV9efXcxPAyYst66ZNF702MYkp6DqFTNxAievYHDeout3kW3NXGv3182At9eARzP_esw6mQd9hZbF9Fm3QangekpIL3RY0B6CmgajQHx_67rgjk</recordid><startdate>20031201</startdate><enddate>20031201</enddate><creator>Gourinath, S.</creator><creator>Himmel, Daniel M.</creator><creator>Brown, Jerry H.</creator><creator>Reshetnikova, Ludmilla</creator><creator>Szent-Györgyi, Andrew G.</creator><creator>Cohen, Carolyn</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>20031201</creationdate><title>Crystal Structure of Scallop Myosin S1 in the Pre-Power Stroke State to 2.6 Å Resolution: Flexibility and Function in the Head</title><author>Gourinath, S. ; Himmel, Daniel M. ; Brown, Jerry H. ; Reshetnikova, Ludmilla ; Szent-Györgyi, Andrew G. ; Cohen, Carolyn</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-e191t-34546a3826e8f1d8f88443ce9db273f91c0d3ae5181478651ef30ea6384c96f53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Actins - chemistry</topic><topic>Animals</topic><topic>Crystallography, X-Ray</topic><topic>Electrons</topic><topic>Models, Molecular</topic><topic>Mollusca</topic><topic>Muscle, Smooth - metabolism</topic><topic>Myosin Subfragments - chemistry</topic><topic>Myosins - chemistry</topic><topic>Nucleic Acid Conformation</topic><topic>Protein Binding</topic><topic>Protein Conformation</topic><topic>Protein Isoforms</topic><topic>Protein Structure, Secondary</topic><topic>Protein Structure, Tertiary</topic><topic>Temperature</topic><topic>Vanadates - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gourinath, S.</creatorcontrib><creatorcontrib>Himmel, Daniel M.</creatorcontrib><creatorcontrib>Brown, Jerry H.</creatorcontrib><creatorcontrib>Reshetnikova, Ludmilla</creatorcontrib><creatorcontrib>Szent-Györgyi, Andrew G.</creatorcontrib><creatorcontrib>Cohen, Carolyn</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Structure (London)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gourinath, S.</au><au>Himmel, Daniel M.</au><au>Brown, Jerry H.</au><au>Reshetnikova, Ludmilla</au><au>Szent-Györgyi, Andrew G.</au><au>Cohen, Carolyn</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystal Structure of Scallop Myosin S1 in the Pre-Power Stroke State to 2.6 Å Resolution: Flexibility and Function in the Head</atitle><jtitle>Structure (London)</jtitle><addtitle>Structure</addtitle><date>2003-12-01</date><risdate>2003</risdate><volume>11</volume><issue>12</issue><spage>1621</spage><epage>1627</epage><pages>1621-1627</pages><issn>0969-2126</issn><eissn>1878-4186</eissn><abstract>We have extended the X-ray structure determination of the complete scallop myosin head in the pre-power stroke state to 2.6 Å resolution, allowing an atomic comparison of the three major (weak actin binding) states of various myosins. We can now account for conformational differences observed in crystal structures in the so-called “pliant region” at the motor domain-lever arm junction between scallop and vertebrate smooth muscle myosins. A hinge, which may contribute to the compliance of the myosin crossbridge, has also been identified for the first time within the regulatory light-chain domain of the lever arm. Analysis of temperature factors of key joints of the motor domain, especially the SH1 helix, provides crystallographic evidence for the existence of the “internally uncoupled” state in diverse isoforms. The agreement between structural and solution studies reinforces the view that the unwinding of the SH1 helix is a part of the cross-bridge cycle in many myosins.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>14656445</pmid><doi>10.1016/j.str.2003.10.013</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0969-2126 |
| ispartof | Structure (London), 2003-12, Vol.11 (12), p.1621-1627 |
| issn | 0969-2126 1878-4186 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_71428504 |
| source | MEDLINE; Cell Press Free Archives; Elsevier ScienceDirect Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Free Full-Text Journals in Chemistry |
| subjects | Actins - chemistry Animals Crystallography, X-Ray Electrons Models, Molecular Mollusca Muscle, Smooth - metabolism Myosin Subfragments - chemistry Myosins - chemistry Nucleic Acid Conformation Protein Binding Protein Conformation Protein Isoforms Protein Structure, Secondary Protein Structure, Tertiary Temperature Vanadates - chemistry |
| title | Crystal Structure of Scallop Myosin S1 in the Pre-Power Stroke State to 2.6 Å Resolution: Flexibility and Function in the Head |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-30T09%3A58%3A53IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Crystal%20Structure%20of%20Scallop%20Myosin%20S1%20in%20the%20Pre-Power%20Stroke%20State%20to%202.6%20%C3%85%20Resolution:%20Flexibility%20and%20Function%20in%20the%20Head&rft.jtitle=Structure%20(London)&rft.au=Gourinath,%20S.&rft.date=2003-12-01&rft.volume=11&rft.issue=12&rft.spage=1621&rft.epage=1627&rft.pages=1621-1627&rft.issn=0969-2126&rft.eissn=1878-4186&rft_id=info:doi/10.1016/j.str.2003.10.013&rft_dat=%3Cproquest_pubme%3E71428504%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=71428504&rft_id=info:pmid/14656445&rft_els_id=S0969212603002569&rfr_iscdi=true |