2l19

From Proteopedia

(Difference between revisions)

Current revision

An arsenate reductase in the intermediate state

Structural highlights

2l19 is a 1 chain structure with sequence from Synechocystis sp. PCC 6803. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR, 20 models
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/2l19"

Categories: Large Structures | Synechocystis sp. PCC 6803 | Jin C | Xia B | Yu C

@@ Line 1: / Line 1: @@
-[[Image:2l19.jpg|left|200px]]
-<!--
+==An arsenate reductase in the intermediate state==
-The line below this paragraph, containing "STRUCTURE_2l19", creates the "Structure Box" on the page.
+<StructureSection load='2l19' size='340' side='right'caption='[[2l19]]' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2l19]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803 Synechocystis sp. PCC 6803]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L19 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L19 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=2l19 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l19 OCA], [https://pdbe.org/2l19 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l19 RCSB], [https://www.ebi.ac.uk/pdbsum/2l19 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l19 ProSAT]</span></td></tr>
-{{STRUCTURE_2l19|  PDB=2l19  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/ARSC_SYNY3 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.<ref>PMID:14617642</ref> <ref>PMID:19304854</ref> <ref>PMID:22155275</ref>
+<div style="background-color:#fffaf0;">
+== 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.
-===An arsenate reductase in the intermediate state===
+(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<ref>PMID:20960080</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2l19" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_20960080}}, adds the Publication Abstract to the page
+*[[Arsenate reductase 3D structures|Arsenate reductase 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 20960080 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_20960080}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-[[2l19]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Synechocystis Synechocystis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L19 OCA].
+[[Category: Synechocystis sp. PCC 6803]]
+[[Category: Jin C]]
-==Reference==
+[[Category: Xia B]]
-<ref group="xtra">PMID:20960080</ref><references group="xtra"/>
+[[Category: Yu C]]
-[[Category: Synechocystis]]
-[[Category: Jin, C.]]
-[[Category: Xia, B.]]
-[[Category: Yu, C.]]

2l19

From Proteopedia

Current revision

An arsenate reductase in the intermediate state

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox