Comparison of the X‐ray structure of native rubredoxin from pyrococcus furiosus with the NMR structure of the zinc‐substituted protein
The three‐dimensional X‐ray structures of the oxidized and reduced forms of rubredoxin from Pyrococcus furiosus, determined at ‐161°C, and the NMR structure of the zinc‐substituted protein, determined in solution at 45°C, are compared. The NMR and X‐ray structures, which were determined independentl...
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| Veröffentlicht in: | Protein science 1992-11, Vol.1 (11), p.1522-1525 |
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| container_issue | 11 |
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| container_title | Protein science |
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| creator | Blake, Paul R. Day, Michael W. Hsu, Barbara T. Joshua‐Tor, Leemor Park, Jae‐Bum Hare, Dennis R. Adams, Michael W. W. Rees, Douglas C. Summers, Michael F. |
| description | The three‐dimensional X‐ray structures of the oxidized and reduced forms of rubredoxin from Pyrococcus furiosus, determined at ‐161°C, and the NMR structure of the zinc‐substituted protein, determined in solution at 45°C, are compared. The NMR and X‐ray structures, which were determined independently, are very similar and lead to similar conclusions regarding the interactions that confer hyperthermostability. |
| doi_str_mv | 10.1002/pro.5560011113 |
| format | Article |
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The NMR and X‐ray structures, which were determined independently, are very similar and lead to similar conclusions regarding the interactions that confer hyperthermostability.</description><subject>Amino Acid Sequence</subject><subject>Archaea - metabolism</subject><subject>Archaebacteria</subject><subject>distance geometry</subject><subject>hyperthermophile</subject><subject>iron‐sulfur protein</subject><subject>Magnetic Resonance Spectroscopy - methods</subject><subject>Marine</subject><subject>Models, Molecular</subject><subject>NMR structure</subject><subject>protein structure</subject><subject>Protein Structure, Secondary</subject><subject>Pyrococcus furiosus</subject><subject>rubredoxin</subject><subject>Rubredoxins - chemistry</subject><subject>Rubredoxins - metabolism</subject><subject>X-Ray Diffraction - methods</subject><subject>X‐ray structure</subject><subject>Zinc - metabolism</subject><subject>zinc substitution</subject><issn>0961-8368</issn><issn>1469-896X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1u1DAUhS0EKtPClh2SV-wy2HHixBskNCotUmlRBVJ3lu3cMEZJHPzTMl2xZsUz8iR4OhVtV70bX_scf_bVQegVJUtKSPl29m5Z15wQmos9QQtacVG0gl88RQsiOC1axtvnaD-E74SQipZsD-1RRljTkAX6vXLjrLwNbsKux3EN-OLvrz9ebXCIPpmYPGyFSUV7Cdgn7aFzP-2Ee-9GPG-8M86YFHCfvHUhN1c2rm9Ap5_OH0K2h9d2MvmBkHSINqYIHc4jRLDTC_SsV0OAl7frAfr64fDL6rg4OTv6uHp_UpiKc1aUDXAGHdGkr9uGgxaUm0ZBpUklOt3ymhlei641glclFQJKUwLnWtdadKxnB-jdjjsnPUJnYIpeDXL2dlR-I52y8qEy2bX85i5lSTOvZBnw5hbg3Y8EIcrRBgPDoCZwKciG1YJl36NGyrmoG9Zk43JnNN6F4KH__xtK5DbmvHfyLuZ84fX9Ge7su1yzLnb6lR1g8whNfj4_u8f-BxVBusA</recordid><startdate>199211</startdate><enddate>199211</enddate><creator>Blake, Paul R.</creator><creator>Day, Michael W.</creator><creator>Hsu, Barbara T.</creator><creator>Joshua‐Tor, Leemor</creator><creator>Park, Jae‐Bum</creator><creator>Hare, Dennis R.</creator><creator>Adams, Michael W. 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W.</au><au>Rees, Douglas C.</au><au>Summers, Michael F.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Comparison of the X‐ray structure of native rubredoxin from pyrococcus furiosus with the NMR structure of the zinc‐substituted protein</atitle><jtitle>Protein science</jtitle><addtitle>Protein Sci</addtitle><date>1992-11</date><risdate>1992</risdate><volume>1</volume><issue>11</issue><spage>1522</spage><epage>1525</epage><pages>1522-1525</pages><issn>0961-8368</issn><eissn>1469-896X</eissn><abstract>The three‐dimensional X‐ray structures of the oxidized and reduced forms of rubredoxin from Pyrococcus furiosus, determined at ‐161°C, and the NMR structure of the zinc‐substituted protein, determined in solution at 45°C, are compared. The NMR and X‐ray structures, which were determined independently, are very similar and lead to similar conclusions regarding the interactions that confer hyperthermostability.</abstract><cop>Bristol</cop><pub>Cold Spring Harbor Laboratory Press</pub><pmid>1303770</pmid><doi>10.1002/pro.5560011113</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
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| ispartof | Protein science, 1992-11, Vol.1 (11), p.1522-1525 |
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| language | eng |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Amino Acid Sequence Archaea - metabolism Archaebacteria distance geometry hyperthermophile iron‐sulfur protein Magnetic Resonance Spectroscopy - methods Marine Models, Molecular NMR structure protein structure Protein Structure, Secondary Pyrococcus furiosus rubredoxin Rubredoxins - chemistry Rubredoxins - metabolism X-Ray Diffraction - methods X‐ray structure Zinc - metabolism zinc substitution |
| title | Comparison of the X‐ray structure of native rubredoxin from pyrococcus furiosus with the NMR structure of the zinc‐substituted protein |
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