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1opd

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(New page: 200px<br /> <applet load="1opd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1opd, resolution 1.5&Aring;" /> '''HISTIDINE-CONTAINING...)
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==About this Structure==
==About this Structure==
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1OPD is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with SO4 as [[http://en.wikipedia.org/wiki/ligand ligand]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OPD OCA]].
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1OPD is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with SO4 as [[http://en.wikipedia.org/wiki/ligand ligand]]. Structure known Active Sites: ACT and AS6. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OPD OCA]].
==Reference==
==Reference==
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[[Category: phosphotransferase]]
[[Category: phosphotransferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 21:06:27 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:48:44 2007''

Revision as of 11:44, 30 October 2007


1opd, resolution 1.5Å

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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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