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1opd
From Proteopedia
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[[Category: phosphotransferase]] | [[Category: phosphotransferase]] | ||
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Revision as of 13:53, 30 October 2007
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HISTIDINE-CONTAINING PROTEIN (HPR), MUTANT WITH SER 46 REPLACED BY ASP (S46D)
Overview
Histidine-containing protein (HPr) is a phosphocarrier protein of the, bacterial phosphoenolpyruvate:sugar phosphotransferase system. HPr is, phosphorylated at the active site residue, His15, by, phosphoenolpyruvate-dependent enzyme I in the first enzyme reaction in the, process of phosphoryl transfer to sugar. In many Gram-positive bacterial, species HPr may also be phosphorylated at Ser46 by an ATP-dependent, protein kinase but not in the Gram-negative Escherichia coli and, Salmonella typhimurium. One effect of the phosphorylation at Ser46 is to, make HPr a poor acceptor for phosphorylation at His15. In Bacillus, subtilis HPr, the mutation Ser46Asp mimics the effects of phosphorylation., A series of mutations were made at Ser46 in E. coli HPr: Ala, Arg, Asn, Asp, Glu, and Gly. The two ... [(full description)]
About this Structure
1OPD is a [Single protein] structure of sequence from [Escherichia coli] with SO4 as [ligand]. Structure known Active Sites: ACT and AS6. Full crystallographic information is available from [OCA].
Reference
Mutation of serine-46 to aspartate in the histidine-containing protein of Escherichia coli mimics the inactivation by phosphorylation of serine-46 in HPrs from gram-positive bacteria., Napper S, Anderson JW, Georges F, Quail JW, Delbaere LT, Waygood EB, Biochemistry. 1996 Sep 3;35(35):11260-7. PMID:8784179
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