1e8j

From Proteopedia

(Difference between revisions)

Revision as of 10:47, 14 July 2021

SOLUTION STRUCTURE OF DESULFOVIBRIO GIGAS ZINC RUBREDOXIN, NMR, 20 STRUCTURES

Structural highlights

1e8j is a 1 chain structure with sequence from Atcc 19364. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[RUBR_DESGI] 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. Electron acceptor for cytoplasmic lactate dehydrogenase.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Rubredoxins are small, soluble proteins that display a wide variation in thermostability, despite having a high degree of sequence similarity They also vary in the extent to which they are stabilized by solutes such as diglycerol phosphate. Hence, they provide excellent models for studying the mechanisms of thermostabilization. Nuclear magnetic resonance (NMR) spectroscopy can be used to investigate interactions between molecules, as well as subtle changes in conformation in solution, and also provides a means to measure protein stability. The assignment of the proton NMR spectrum of the zinc rubredoxin from Desulfovibrio gigas is presented, together with its structure in solution. The stabilizing effect of diglycerol phosphate on rubredoxin is demonstrated and assessed by determining selected amide proton exchange rates; diglycerol phosphate at 100 mM concentration caused an additional structural stabilization of 1.2 +/-0.4 kJ/mol. The pattern of effects on the exchange rates is discussed in relation to the protein structure.

NMR structure of Desulfovibrio gigas rubredoxin: a model for studying protein stabilization by compatible solutes.,Lamosa P, Brennan L, Vis H, Turner DL, Santos H Extremophiles. 2001 Oct;5(5):303-11. PMID:11699644^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Lamosa P, Brennan L, Vis H, Turner DL, Santos H. NMR structure of Desulfovibrio gigas rubredoxin: a model for studying protein stabilization by compatible solutes. Extremophiles. 2001 Oct;5(5):303-11. PMID:11699644

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1e8j"

@@ Line 3: / Line 3: @@
 <StructureSection load='1e8j' size='340' side='right'caption='[[1e8j]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1e8j]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_19364 Atcc 19364]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E8J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E8J FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1e8j]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_19364 Atcc 19364]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E8J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E8J FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e8j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e8j OCA], [http://pdbe.org/1e8j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e8j RCSB], [http://www.ebi.ac.uk/pdbsum/1e8j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1e8j ProSAT]</span></td></tr>
+</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=1e8j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e8j OCA], [https://pdbe.org/1e8j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e8j RCSB], [https://www.ebi.ac.uk/pdbsum/1e8j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e8j ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/RUBR_DESGI RUBR_DESGI]] 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.  Electron acceptor for cytoplasmic lactate dehydrogenase.
+[[https://www.uniprot.org/uniprot/RUBR_DESGI RUBR_DESGI]] 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.  Electron acceptor for cytoplasmic lactate dehydrogenase.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1e8j

From Proteopedia

Revision as of 10:47, 14 July 2021

SOLUTION STRUCTURE OF DESULFOVIBRIO GIGAS ZINC RUBREDOXIN, NMR, 20 STRUCTURES

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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