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2l18

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Revision as of 08:34, 25 July 2018

An arsenate reductase in the phosphate binding state

Structural highlights

2l18 is a 1 chain structure with sequence from Aphanocapsa sp. (strain n-1). Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	2l17, 2l19
Gene:	arsC, slr0946 (Aphanocapsa sp. (strain N-1))
Activity:	Arsenate reductase (glutaredoxin), with EC number 1.20.4.1
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ARSC_SYNY3] Reduces arsenate [As(V)] to arsenite [As(III)] using glutathione and glutaredoxin as sources of reducing equivalents. GrxA is the most effective electron donor in vivo compared to other glutaredoxins. Constitutes the major arsenate reductase compared to ArsI1 and ArsI2. Also shows weak phosphatase activity toward p-nitrophenyl phosphate.^[1] ^[2] ^[3]

Publication Abstract from PubMed

Arsenate reductases (ArsC) are a group of enzymes that play essential roles in biological arsenic detoxification pathways by catalyzing the intracellular reduction of arsenate to arsenite, which is subsequently extruded from the cells by specific transport systems. The ArsC protein from cyanobacterium Synechocystis sp. strain PCC 6803 (SynArsC) is related to the thioredoxin-dependent ArsC family, but uses the glutathione/glutaredoxin system for arsenate reduction. Therefore, it is classified to a novel thioredoxin/glutaredoxin hybrid arsenate reductase family. Herein we report the chemical shift assignments of (1)H, (13)C and (15)N atoms for the reduced form of SynArsC, which provides a starting point for further structural analysis and elucidation of its enzymatic mechanism.

(1)H, (13)C and (15)N resonance assignments of the arsenate reductase from Synechocystis sp. strain PCC 6803.,Yu C, Xia B, Jin C Biomol NMR Assign. 2011 Apr;5(1):85-7. Epub 2010 Oct 20. PMID:20960080^[4]

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

References

↑ Li R, Haile JD, Kennelly PJ. An arsenate reductase from Synechocystis sp. strain PCC 6803 exhibits a novel combination of catalytic characteristics. J Bacteriol. 2003 Dec;185(23):6780-9. PMID:14617642
↑ Lopez-Maury L, Sanchez-Riego AM, Reyes JC, Florencio FJ. The glutathione/glutaredoxin system is essential for arsenate reduction in Synechocystis sp. strain PCC 6803. J Bacteriol. 2009 Jun;191(11):3534-43. doi: 10.1128/JB.01798-08. Epub 2009 Mar, 20. PMID:19304854 doi:http://dx.doi.org/10.1128/JB.01798-08
↑ Kim SG, Chung JS, Sutton RB, Lee JS, Lopez-Maury L, Lee SY, Florencio FJ, Lin T, Zabet-Moghaddam M, Wood MJ, Nayak K, Madem V, Tripathy JN, Kim SK, Knaff DB. Redox, mutagenic and structural studies of the glutaredoxin/arsenate reductase couple from the cyanobacterium Synechocystis sp. PCC 6803. Biochim Biophys Acta. 2012 Feb;1824(2):392-403. Epub 2011 Oct 29. PMID:22155275 doi:10.1016/j.bbapap.2011.10.012
↑ Yu C, Xia B, Jin C. (1)H, (13)C and (15)N resonance assignments of the arsenate reductase from Synechocystis sp. strain PCC 6803. Biomol NMR Assign. 2011 Apr;5(1):85-7. Epub 2010 Oct 20. PMID:20960080 doi:10.1007/s12104-010-9273-2

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2l18"

Categories: Jin, C | Xia, B | Yu, C | Alpha/beta sandwich | Oxidoreductase

@@ Line 1: / Line 1: @@
 ==An arsenate reductase in the phosphate binding state==
 <StructureSection load='2l18' size='340' side='right' caption='[[2l18]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">arsC, slr0946 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1148 Aphanocapsa sp. (strain N-1)])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Arsenate_reductase_(glutaredoxin) Arsenate reductase (glutaredoxin)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.20.4.1 1.20.4.1] </span></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=2l18 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l18 OCA], [http://pdbe.org/2l18 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2l18 RCSB], [http://www.ebi.ac.uk/pdbsum/2l18 PDBsum]</span></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=2l18 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l18 OCA], [http://pdbe.org/2l18 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2l18 RCSB], [http://www.ebi.ac.uk/pdbsum/2l18 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2l18 ProSAT]</span></td></tr>
 </table>
 == Function ==

2l18

From Proteopedia

Revision as of 08:34, 25 July 2018

An arsenate reductase in the phosphate binding state

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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