1qcv

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==RUBREDOXIN VARIANT (PFRD-XC4) FOLDS WITHOUT IRON==
==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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<StructureSection load='1qcv' size='340' side='right'caption='[[1qcv]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1qcv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43587 Atcc 43587]. 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 [https://proteopedia.org/fgij/fg.htm?mol=1QCV FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1qcv]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=1QCV FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qcv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qcv OCA], [https://pdbe.org/1qcv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qcv RCSB], [https://www.ebi.ac.uk/pdbsum/1qcv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qcv ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qcv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qcv OCA], [https://pdbe.org/1qcv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qcv RCSB], [https://www.ebi.ac.uk/pdbsum/1qcv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qcv ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/RUBR_PYRFU RUBR_PYRFU]] Rubredoxin is a small nonheme, iron protein lacking acid-labile sulfide. Its single Fe, chelated to 4 Cys, functions as an electron acceptor and may also stabilize the conformation of the molecule.
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[https://www.uniprot.org/uniprot/RUBR_PYRFU RUBR_PYRFU] Rubredoxin is a small nonheme, iron protein lacking acid-labile sulfide. Its single Fe, chelated to 4 Cys, functions as an electron acceptor and may also stabilize the conformation of the molecule.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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/main_output.php?pdb_ID=1qcv ConSurf].
</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/main_output.php?pdb_ID=1qcv ConSurf].
<div style="clear:both"></div>
<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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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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==See Also==
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*[[Rubredoxin 3D structures|Rubredoxin 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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*[[Rubredoxin PDB structures|Rubredoxin PDB structures]]
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</div>
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<div class="pdbe-citations 1qcv" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 43587]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Mayo, S L]]
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[[Category: Pyrococcus furiosus]]
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[[Category: Strop, P]]
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[[Category: Mayo SL]]
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[[Category: Electron transport]]
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[[Category: Strop P]]
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[[Category: Hyperthermophile]]
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[[Category: Rubredoxin]]
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Current revision

RUBREDOXIN VARIANT (PFRD-XC4) FOLDS WITHOUT IRON

PDB ID 1qcv

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