NDLI: The Transport/Phosphorylation ofN,N′-Diacetylchitobiose in Escherichia coli CHARACTERIZATION OF PHOSPHO-IIBChb AND OF A POTENTIAL TRANSITION STATE ANALOGUE IN THE PHOSPHOTRANSFER REACTION BETWEEN THE PROTEINS IIAChb AND IIBChb

Content Provider	Journal of Biological Chemistry (JBC)
Author	Keyhani, Nemat O. Bacia, Kirsten Roseman, Saul
Abstract	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. IIBChb 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 IIBChb mutant (C10S) have been reported. In the present studies, homogeneous phospho-IIBChb was isolated, and the phosphoryl-Cys linkage was established by 31P NMR spectroscopy. Rate constants for the hydrolysis of phospho-IIBChb plotted versuspH 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 Cys10SerIIBChb (which cannot be phosphorylated) and phospho-IIAChb, but not with IIAChb. 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-IIAChb + IIBChb ↔ IIAChb+ phospho-IIBChb. This is apparently the first report of the isolation of a transition state analogue in a protein-protein phosphotransfer reaction.
Related Links	http://www.jbc.org/content/275/42/33102.abstract
Ending Page	33109
Starting Page	33102
Page Count	8
File Format	HTM / HTML PDF
ISSN	00219258
Journal	Journal of Biological Chemistry (JBC)
Issue Number	42
Volume Number	275
DOI	10.1074/jbc.M001045200
e-ISSN	1083351X
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	2000-10-20
Access Restriction	Open
Subject Keyword	Β-1,4-linked oligomers of GlcNAc wheren = 2–6 ((GlcNAc)n) Phosphoenolpyruvate:glycose phosphotransferase system (PTS) Dithiothreitol (DTT) Polyacrylamide gel electrophoresis (PAGE) 4-morpholinepropanesulfonic acid (MOPS) 3-{[2-hydroxy-1,1-bis(hydroxymethyl)ethyl]amino}-1-propanesulfonic acid (TAPS) Phosphoenolpyruvate (PEP) Bis(sulfosuccinimidyl)suberate (BS3) 3,3′-dithiobis(sulfosuccinimidyl proprionate) (DTSSP) MEMBRANE TRANSPORT STRUCTURE FUNCTION AND BIOGENESIS
Alternative Title	The Transport/Phosphorylation ofN,N′-Diacetylchitobiose in Escherichia coli
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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Analytical Sedimentation of the IIAChb and IIBChb Proteins of the Escherichia coli N,N′-Diacetylchitobiose Phosphotransferase System DEMONSTRATION OF A MODEL PHOSPHOTRANSFER TRANSITION STATE COMPLEX

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