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1rwd

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Revision as of 15:28, 27 October 2021

Backbone NMR Structure of a Mutant P. Furiosus Rubredoxin Using Residual Dipolar Couplings

Structural highlights

1rwd is a 1 chain structure with sequence from Atcc 43587. This structure supersedes the now removed PDB entry 1m2y. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1m2y
Gene:	RUB, PF1282 (ATCC 43587)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

[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

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

Publication Abstract from PubMed

A new approach for simultaneous protein backbone resonance assignment and structure determination by NMR is introduced. This approach relies on recent advances in high-resolution NMR spectroscopy that allow observation of anisotropic interactions, such as dipolar couplings, from proteins partially aligned in field ordered media. Residual dipolar couplings are used for both geometric information and a filter in the assembly of residues in a sequential manner. Experimental data were collected in less than one week on a small redox protein, rubredoxin, that was 15N enriched but not enriched above 1% natural abundance in 13C. Given the acceleration possible with partial 13C enrichment, the protocol described should provide a very rapid route to protein structure determination. This is critical for the structural genomics initiative where protein expression and structural determination in a high-throughput manner will be needed.

A dipolar coupling based strategy for simultaneous resonance assignment and structure determination of protein backbones.,Tian F, Valafar H, Prestegard JH J Am Chem Soc. 2001 Nov 28;123(47):11791-6. PMID:11716736^[1]

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

References

↑ Tian F, Valafar H, Prestegard JH. A dipolar coupling based strategy for simultaneous resonance assignment and structure determination of protein backbones. J Am Chem Soc. 2001 Nov 28;123(47):11791-6. PMID:11716736

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/1rwd"

@@ Line 3: / Line 3: @@
 <StructureSection load='1rwd' size='340' side='right'caption='[[1rwd]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1rwd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43587 Atcc 43587]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1m2y 1m2y]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RWD OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1RWD FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1rwd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43587 Atcc 43587]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1m2y 1m2y]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RWD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RWD FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1m2y|1m2y]]</div></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RUB, PF1282 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2261 ATCC 43587])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RUB, PF1282 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2261 ATCC 43587])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1rwd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rwd OCA], [http://pdbe.org/1rwd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rwd RCSB], [http://www.ebi.ac.uk/pdbsum/1rwd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1rwd ProSAT], [http://www.topsan.org/Proteins/SECSG/1rwd TOPSAN]</span></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=1rwd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rwd OCA], [https://pdbe.org/1rwd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rwd RCSB], [https://www.ebi.ac.uk/pdbsum/1rwd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rwd ProSAT], [https://www.topsan.org/Proteins/SECSG/1rwd TOPSAN]</span></td></tr>
 </table>
 == Function ==
-[[http://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 ==
 [[Image:Consurf_key_small.gif|200px|right]]

1rwd

From Proteopedia

Revision as of 15:28, 27 October 2021

Backbone NMR Structure of a Mutant P. Furiosus Rubredoxin Using Residual Dipolar Couplings

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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