Linked Life Data

10433726

Source:http://linkedlifedata.com/resource/pubmed/id/10433726

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
31
pubmed:dateCreated
1999-9-3
pubmed:abstractText
Resistance to several toxic anions in Escherichia coli is conferred by the ars operon carried on plasmid R773. The gene products of this operon catalyze extrusion of antimonials and arsenicals from cells. In this paper, we report the determination of the overall fold for ArsC, a 16 kDa protein of the ars operon involved in the reduction of arsenate to arsenite, using multidimensional, multinuclear NMR. The protein is found to contain large regions of extensive mobility, particularly in the active site. A model fold, computed on the basis of a preliminary set of NOEs, was found to be structurally homologous to E. coli glutaredoxin, thiol transferases, and glutathione S-transferase. Some kinship to the structure of low molecular weight tyrosine phosphatases, based on rough topological similarity but more so on the basis of a common anion-binding-loop motif H-CX(n)R, was also detected. Although functional, secondary, and tertiary structural homology is observed with these molecules, no significant homology in primary structure was detected. The mobilities of the active site of ArsC and of other enzymes are discussed.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
3
pubmed:volume
38
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
10178-86
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:10433726-Adenosine Triphosphatases, pubmed-meshheading:10433726-Amino Acid Sequence, pubmed-meshheading:10433726-Arsenic, pubmed-meshheading:10433726-Arsenite Transporting ATPases, pubmed-meshheading:10433726-Binding Sites, pubmed-meshheading:10433726-Drug Resistance, Microbial, pubmed-meshheading:10433726-Escherichia coli, pubmed-meshheading:10433726-Ion Pumps, pubmed-meshheading:10433726-Molecular Sequence Data, pubmed-meshheading:10433726-Multienzyme Complexes, pubmed-meshheading:10433726-Nuclear Magnetic Resonance, Biomolecular, pubmed-meshheading:10433726-Oxidation-Reduction, pubmed-meshheading:10433726-Plasmids, pubmed-meshheading:10433726-Protein Folding, pubmed-meshheading:10433726-Protein Structure, Secondary, pubmed-meshheading:10433726-Sequence Homology, Amino Acid
pubmed:year
1999
pubmed:articleTitle
Secondary structure and fold homology of the ArsC protein from the Escherichia coli arsenic resistance plasmid R773.
pubmed:affiliation
Biophysics Research Division, Department of Biological Chemistry, University of Michigan, Ann Arbor 48109-1055, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't