1qcv: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
 
Line 1: Line 1:


==RUBREDOXIN VARIANT (PFRD-XC4) FOLDS WITHOUT IRON==
==RUBREDOXIN VARIANT (PFRD-XC4) FOLDS WITHOUT IRON==
<StructureSection load='1qcv' size='340' side='right'caption='[[1qcv]], [[NMR_Ensembles_of_Models | 29 NMR models]]' scene=''>
<StructureSection load='1qcv' size='340' side='right'caption='[[1qcv]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<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>
<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>
</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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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>
</table>
</table>
== Function ==
== Function ==
[[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.  
[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]]
Line 18: Line 19:
</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>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


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>
==See Also==
 
*[[Rubredoxin 3D structures|Rubredoxin 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
*[[Rubredoxin PDB structures|Rubredoxin PDB structures]]
</div>
<div class="pdbe-citations 1qcv" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 43587]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Mayo, S L]]
[[Category: Pyrococcus furiosus]]
[[Category: Strop, P]]
[[Category: Mayo SL]]
[[Category: Electron transport]]
[[Category: Strop P]]
[[Category: Hyperthermophile]]
[[Category: Rubredoxin]]

Latest revision as of 06:03, 17 April 2024

RUBREDOXIN VARIANT (PFRD-XC4) FOLDS WITHOUT IRON

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1qcv&oldid=4129912"