Structures and Analysis of Highly Homologous Psychrophilic, Mesophilic, and Thermophilic Adenylate Kinases
The crystal structures of adenylate kinases from the psychrophile Bacillus globisporus and the mesophile Bacillus subtilis have been solved and compared with that from the thermophile Bacillus stearothermophilus . This is the first example we know of where a trio of protein structures has been solve...
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| Veröffentlicht in: | The Journal of biological chemistry 2004-07, Vol.279 (27), p.28202-28208 |
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| container_title | The Journal of biological chemistry |
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| creator | Bae, Euiyoung Phillips, Jr, George N |
| description | The crystal structures of adenylate kinases from the psychrophile Bacillus globisporus and the mesophile Bacillus subtilis have been solved and compared with that from the thermophile Bacillus stearothermophilus . This is the first example we know of where a trio of protein structures has been solved that have the same number of amino
acids and a high level of identity (66â74%) and yet come from organisms with different operating temperatures. The enzymes
were characterized for their own thermal denaturation and inactivation, and they exhibited the same temperature preferences
as their source organisms. The structures of the three highly homologous, dynamic proteins with different temperature-activity
profiles provide an opportunity to explore a molecular mechanism of cold and heat adaptation. Their analysis suggests that
the maintenance of the balance between stability and flexibility is crucial for proteins to function at their environmental
temperatures, and it is achieved by the modification of intramolecular interactions in the process of temperature adaptation. |
| doi_str_mv | 10.1074/jbc.M401865200 |
| format | Article |
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acids and a high level of identity (66â74%) and yet come from organisms with different operating temperatures. The enzymes
were characterized for their own thermal denaturation and inactivation, and they exhibited the same temperature preferences
as their source organisms. The structures of the three highly homologous, dynamic proteins with different temperature-activity
profiles provide an opportunity to explore a molecular mechanism of cold and heat adaptation. Their analysis suggests that
the maintenance of the balance between stability and flexibility is crucial for proteins to function at their environmental
temperatures, and it is achieved by the modification of intramolecular interactions in the process of temperature adaptation.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M401865200</identifier><identifier>PMID: 15100224</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Adenylate Kinase - chemistry ; Amino Acid Sequence ; Bacillus - enzymology ; Bacillus globisporus ; Bacillus stearothermophilus ; Bacillus subtilis ; Bacillus subtilis - enzymology ; Calorimetry, Differential Scanning ; Cloning, Molecular ; Cold Temperature ; Crystallography, X-Ray ; Escherichia coli - metabolism ; Geobacillus stearothermophilus - enzymology ; Hot Temperature ; Hydrogen Bonding ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Sequence Homology, Amino Acid ; Species Specificity ; Temperature ; Zinc - chemistry</subject><ispartof>The Journal of biological chemistry, 2004-07, Vol.279 (27), p.28202-28208</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c457t-6ba3b83ec79a294dda814c7c9726a7fb863b02605709ebd6af4d25c10f3db1f33</citedby><cites>FETCH-LOGICAL-c457t-6ba3b83ec79a294dda814c7c9726a7fb863b02605709ebd6af4d25c10f3db1f33</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27923,27924</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15100224$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bae, Euiyoung</creatorcontrib><creatorcontrib>Phillips, Jr, George N</creatorcontrib><title>Structures and Analysis of Highly Homologous Psychrophilic, Mesophilic, and Thermophilic Adenylate Kinases</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>The crystal structures of adenylate kinases from the psychrophile Bacillus globisporus and the mesophile Bacillus subtilis have been solved and compared with that from the thermophile Bacillus stearothermophilus . This is the first example we know of where a trio of protein structures has been solved that have the same number of amino
acids and a high level of identity (66â74%) and yet come from organisms with different operating temperatures. The enzymes
were characterized for their own thermal denaturation and inactivation, and they exhibited the same temperature preferences
as their source organisms. The structures of the three highly homologous, dynamic proteins with different temperature-activity
profiles provide an opportunity to explore a molecular mechanism of cold and heat adaptation. Their analysis suggests that
the maintenance of the balance between stability and flexibility is crucial for proteins to function at their environmental
temperatures, and it is achieved by the modification of intramolecular interactions in the process of temperature adaptation.</description><subject>Adenylate Kinase - chemistry</subject><subject>Amino Acid Sequence</subject><subject>Bacillus - enzymology</subject><subject>Bacillus globisporus</subject><subject>Bacillus stearothermophilus</subject><subject>Bacillus subtilis</subject><subject>Bacillus subtilis - enzymology</subject><subject>Calorimetry, Differential Scanning</subject><subject>Cloning, Molecular</subject><subject>Cold Temperature</subject><subject>Crystallography, X-Ray</subject><subject>Escherichia coli - metabolism</subject><subject>Geobacillus stearothermophilus - enzymology</subject><subject>Hot Temperature</subject><subject>Hydrogen Bonding</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Protein Conformation</subject><subject>Sequence Homology, Amino Acid</subject><subject>Species Specificity</subject><subject>Temperature</subject><subject>Zinc - chemistry</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkctLJDEQh4O46Pi4epQcZE_2bB7deRwH2d2RVXZBBW8hSaftDN2dMelG-r_fyAx6tKCoouqrgqofABcYLTHi5Y-Nscv7EmHBKoLQAVhgJGhBK_x8CBYIEVxIUoljcJLSBmUrJT4Cx7jCuUfKBdg8jHGy4xRdgnqo4WrQ3Zx8gqGBa__SdjNchz504SVMCf5Ls21j2La-8_Ya3rv0kb8PP7Yu9vsKXNVumDs9OvjHDzq5dAa-NbpL7nwfT8HTr5-PN-vi7u_v25vVXWHLio8FM5oaQZ3lUhNZ1rUWuLTcSk6Y5o0RjBpEGKo4ks7UTDdlTSqLUUNrgxtKT8H33d5tDK-TS6PqfbKu6_Tg8hGKMVZxKfCXIOaCYE5lBpc70MaQUnSN2kbf6zgrjNS7DCrLoD5lyAOX-82T6V39ie__noGrHdDmH7_56JTxwbauV4TL7IoIggj9D7tmkGU</recordid><startdate>20040702</startdate><enddate>20040702</enddate><creator>Bae, Euiyoung</creator><creator>Phillips, Jr, George N</creator><general>American Society for Biochemistry and Molecular Biology</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>20040702</creationdate><title>Structures and Analysis of Highly Homologous Psychrophilic, Mesophilic, and Thermophilic Adenylate Kinases</title><author>Bae, Euiyoung ; Phillips, Jr, George N</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c457t-6ba3b83ec79a294dda814c7c9726a7fb863b02605709ebd6af4d25c10f3db1f33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Adenylate Kinase - chemistry</topic><topic>Amino Acid Sequence</topic><topic>Bacillus - enzymology</topic><topic>Bacillus globisporus</topic><topic>Bacillus stearothermophilus</topic><topic>Bacillus subtilis</topic><topic>Bacillus subtilis - enzymology</topic><topic>Calorimetry, Differential Scanning</topic><topic>Cloning, Molecular</topic><topic>Cold Temperature</topic><topic>Crystallography, X-Ray</topic><topic>Escherichia coli - metabolism</topic><topic>Geobacillus stearothermophilus - enzymology</topic><topic>Hot Temperature</topic><topic>Hydrogen Bonding</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Protein Conformation</topic><topic>Sequence Homology, Amino Acid</topic><topic>Species Specificity</topic><topic>Temperature</topic><topic>Zinc - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bae, Euiyoung</creatorcontrib><creatorcontrib>Phillips, Jr, George N</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bae, Euiyoung</au><au>Phillips, Jr, George N</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structures and Analysis of Highly Homologous Psychrophilic, Mesophilic, and Thermophilic Adenylate Kinases</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2004-07-02</date><risdate>2004</risdate><volume>279</volume><issue>27</issue><spage>28202</spage><epage>28208</epage><pages>28202-28208</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>The crystal structures of adenylate kinases from the psychrophile Bacillus globisporus and the mesophile Bacillus subtilis have been solved and compared with that from the thermophile Bacillus stearothermophilus . This is the first example we know of where a trio of protein structures has been solved that have the same number of amino
acids and a high level of identity (66â74%) and yet come from organisms with different operating temperatures. The enzymes
were characterized for their own thermal denaturation and inactivation, and they exhibited the same temperature preferences
as their source organisms. The structures of the three highly homologous, dynamic proteins with different temperature-activity
profiles provide an opportunity to explore a molecular mechanism of cold and heat adaptation. Their analysis suggests that
the maintenance of the balance between stability and flexibility is crucial for proteins to function at their environmental
temperatures, and it is achieved by the modification of intramolecular interactions in the process of temperature adaptation.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>15100224</pmid><doi>10.1074/jbc.M401865200</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Adenylate Kinase - chemistry Amino Acid Sequence Bacillus - enzymology Bacillus globisporus Bacillus stearothermophilus Bacillus subtilis Bacillus subtilis - enzymology Calorimetry, Differential Scanning Cloning, Molecular Cold Temperature Crystallography, X-Ray Escherichia coli - metabolism Geobacillus stearothermophilus - enzymology Hot Temperature Hydrogen Bonding Models, Molecular Molecular Sequence Data Protein Conformation Sequence Homology, Amino Acid Species Specificity Temperature Zinc - chemistry |
| title | Structures and Analysis of Highly Homologous Psychrophilic, Mesophilic, and Thermophilic Adenylate Kinases |
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