2y75

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Revision as of 09:21, 10 October 2018

The Structure of CymR (YrzC) the Global Cysteine Regulator of B. subtilis

Structural highlights

2y75 is a 6 chain structure with sequence from "vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CYMR_BACSU] Master repressor of cysteine metabolism in B.subtilis. Controls the expression of genes involved either in cysteine synthesis from sulfide (cysK), sulfonates (ssu), or methionine (mccAB) or in cystine uptake (tcyP). Activity of CymR is positively regulated by CysK in response to cysteine availability. When cysteine is present, the pool of O-acetylserine (OAS) is low, which leads to the formation of a CymR-CysK complex and transcriptional repression of the CymR regulon occurs. In the absence of cysteine, the OAS pool is high and the CymR-CysK complex is mostly dissociated, leading to a faster dissociation of CymR from its DNA targets and the lifting of CymR-dependent repression.^[1] ^[2]

Publication Abstract from PubMed

The global regulator CymR represses the transcription of a large set of genes involved in cystine uptake and cysteine biosynthesis in Bacillus subtilis and Staphylococcus aureus. This repressor belongs to the widespread and poorly characterized Rrf2 family of regulators. The crystal structure of CymR from B. subtilis reveals a biologically active dimer, where each monomer folds into two tightly packed domains: a DNA-binding domain, which houses a winged helix-turn-helix (wHTH) motif; and a long dimerization domain, which places the wHTH motifs at the extremes. This architecture explains how these small regulators can span 23-27-bp DNA targets. The wHTH motif of CymR resembles those of the GntR superfamily of regulators, such as FadR and HutC. Superimposing the FadR wHTH motifs bound to their DNA fragments onto the wHTH motifs of the CymR dimer structure suggests that the DNA target and/or the protein must undergo some conformational changes upon binding. The CymR structure also hints at a possible location of the Fe-S centre associated with several Rrf2-type regulators. Structured digital abstract * CymR binds to CymR by x-ray crystallography (View Interaction 1, 2).

Insights into the Rrf2 repressor family - the structure of CymR, the global cysteine regulator of Bacillus subtilis.,Shepard W, Soutourina O, Courtois E, England P, Haouz A, Martin-Verstraete I FEBS J. 2011 Aug;278(15):2689-701. doi: 10.1111/j.1742-4658.2011.08195.x., Epub 2011 Jul 1. PMID:21624051^[3]

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

References

↑ Even S, Burguiere P, Auger S, Soutourina O, Danchin A, Martin-Verstraete I. Global control of cysteine metabolism by CymR in Bacillus subtilis. J Bacteriol. 2006 Mar;188(6):2184-97. PMID:16513748 doi:http://dx.doi.org/10.1128/JB.188.6.2184-2197.2006
↑ Tanous C, Soutourina O, Raynal B, Hullo MF, Mervelet P, Gilles AM, Noirot P, Danchin A, England P, Martin-Verstraete I. The CymR regulator in complex with the enzyme CysK controls cysteine metabolism in Bacillus subtilis. J Biol Chem. 2008 Dec 19;283(51):35551-60. Epub 2008 Oct 29. PMID:18974048 doi:http://dx.doi.org/M805951200
↑ Shepard W, Soutourina O, Courtois E, England P, Haouz A, Martin-Verstraete I. Insights into the Rrf2 repressor family - the structure of CymR, the global cysteine regulator of Bacillus subtilis. FEBS J. 2011 Aug;278(15):2689-701. doi: 10.1111/j.1742-4658.2011.08195.x., Epub 2011 Jul 1. PMID:21624051 doi:10.1111/j.1742-4658.2011.08195.x

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2y75"

@@ Line 1: / Line 1: @@
-==THE STRUCTURE OF CYMR (YRZC) THE GLOBAL CYSTEINE REGULATOR OF B. SUBTILIS==
+==The Structure of CymR (YrzC) the Global Cysteine Regulator of B. subtilis==
 <StructureSection load='2y75' size='340' side='right' caption='[[2y75]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2y75]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y75 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2Y75 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2y75]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y75 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2Y75 FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=2y75 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y75 OCA], [http://pdbe.org/2y75 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2y75 RCSB], [http://www.ebi.ac.uk/pdbsum/2y75 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2y75 ProSAT]</span></td></tr>
@@ Line 22: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Bacillus globigii migula 1900]]
+[[Category: Vibrio subtilis ehrenberg 1835]]
 [[Category: Courtois, E]]
 [[Category: England, P]]

2y75

From Proteopedia

Revision as of 09:21, 10 October 2018

The Structure of CymR (YrzC) the Global Cysteine Regulator of B. subtilis

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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