Linked Life Data

10913119

Source:http://linkedlifedata.com/resource/pubmed/id/10913119

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
42
pubmed:dateCreated
2000-11-20
pubmed:abstractText
Enzyme II permeases of the phosphoenolpyruvate:glycose phosphotransferase system comprise one to five separately encoded polypeptides, but most contain similar domains (IIA, IIB, and IIC). The phosphoryl group is transferred from one domain to another, with histidine as the phosphoryl acceptor in IIA and cysteine as the acceptor in certain IIB domains. IIB(Chb) is a phosphocarrier in the uptake/phosphorylation of the chitin disaccharide, (GlcNAc)(2) by Escherichia coli and is unusual because it is separately encoded and soluble. Both the crystal and solution structures of a IIB(Chb) mutant (C10S) have been reported. In the present studies, homogeneous phospho-IIB(Chb) was isolated, and the phosphoryl-Cys linkage was established by (31)P NMR spectroscopy. Rate constants for the hydrolysis of phospho-IIB(Chb) plotted versus pH gave the same shape peak reported for the model compound, butyl thiophosphate, but was shifted about 4 pH units. Evidence is presented for a stable complex between homogeneous Cys10SerIIB(Chb) (which cannot be phosphorylated) and phospho-IIA(Chb), but not with IIA(Chb). The complex (a tetramer (3)) contains equimolar quantities of the two proteins and has been chemically cross-linked. It appears to be an analogue of the transition state complex in the reaction: phospho-IIA(Chb) + IIB(Chb) <--> IIA(Chb) + phospho-IIB(Chb). This is apparently the first report of the isolation of a transition state analogue in a protein-protein phosphotransfer reaction.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
275
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
33102-9
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
The transport/phosphorylation of N,N'-diacetylchitobiose in Escherichia coli. Characterization of phospho-IIB(Chb) and of a potential transition state analogue in the phosphotransfer reaction between the proteins IIA(Chb) AND IIB(Chb).
pubmed:affiliation
Department of Biology and the McCollum-Pratt Institute, The Johns Hopkins University, Baltimore, Maryland 21218, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.