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2L19

An arsenate reductase in the intermediate state

Summary for 2L19
Entry DOI10.2210/pdb2l19/pdb
Related2L17 2L18
DescriptorArsenate reductase (1 entity in total)
Functional Keywordsalpha/beta sandwich, oxidoreductase
Biological sourceSynechocystis
Total number of polymer chains1
Total formula weight14691.52
Authors
Yu, C.,Xia, B.,Jin, C. (deposition date: 2010-07-26, release date: 2011-04-13, Last modification date: 2024-10-30)
Primary citationYu, 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., 5:85-87, 2011
Cited by
PubMed Abstract: 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.
PubMed: 20960080
DOI: 10.1007/s12104-010-9273-2
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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