1qcv

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[[Image:1qcv.png|left|200px]]
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==RUBREDOXIN VARIANT (PFRD-XC4) FOLDS WITHOUT IRON==
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<StructureSection load='1qcv' size='340' side='right' caption='[[1qcv]], [[NMR_Ensembles_of_Models | 29 NMR models]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1qcv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QCV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QCV FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qcv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qcv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1qcv RCSB], [http://www.ebi.ac.uk/pdbsum/1qcv PDBsum]</span></td></tr>
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<table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qc/1qcv_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The role of surface salt bridges in protein stabilization has been a source of controversy. Here we present the NMR structure of a hyperthermophilic rubredoxin variant (PFRD-XC4) and the thermodynamic analysis of two surface salt bridges by double mutant cycles. This analysis shows that the surface side chain to side chain salt bridge between Lys 6 and Glu 49 does not stabilize PFRD-XC4. The main chain to side chain salt bridge between the N-terminus and Glu 14 was, however, found to stabilize PFRD-XC4 by 1. 5 kcal mol(-)(1). The entropic cost of making a surface salt bridge involving the protein's backbone is reduced, since the backbone has already been immobilized upon protein folding.
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{{STRUCTURE_1qcv| PDB=1qcv | SCENE= }}
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Contribution of surface salt bridges to protein stability.,Strop P, Mayo SL Biochemistry. 2000 Feb 15;39(6):1251-5. PMID:10684603<ref>PMID:10684603</ref>
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===RUBREDOXIN VARIANT (PFRD-XC4) FOLDS WITHOUT IRON===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_10684603}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[1qcv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QCV OCA].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:010684603</ref><references group="xtra"/>
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[[Category: Pyrococcus furiosus]]
[[Category: Pyrococcus furiosus]]
[[Category: Mayo, S L.]]
[[Category: Mayo, S L.]]

Revision as of 14:23, 29 September 2014

RUBREDOXIN VARIANT (PFRD-XC4) FOLDS WITHOUT IRON

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