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2lgs

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{{STRUCTURE_2lgs| PDB=2lgs | SCENE= }}
{{STRUCTURE_2lgs| PDB=2lgs | SCENE= }}
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'''FEEDBACK INHIBITION OF FULLY UNADENYLYLATED GLUTAMINE SYNTHETASE FROM SALMONELLA TYPHIMURIUM BY GLYCINE, ALANINE, AND SERINE'''
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===FEEDBACK INHIBITION OF FULLY UNADENYLYLATED GLUTAMINE SYNTHETASE FROM SALMONELLA TYPHIMURIUM BY GLYCINE, ALANINE, AND SERINE===
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==Overview==
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Bacterial glutamine synthetase (GS; EC 6.3.1.2) was previously shown to be inhibited by nine end products of glutamine metabolism. Here we present four crystal structures of GS, complexed with the substrate Glu and with each of three feedback inhibitors. The GS of the present study is from Salmonella typhimurium, with Mn2+ ions bound, and is fully unadenylylated. From Fourier difference maps, we find that L-serine, L-alanine, and glycine bind at the site of the substrate L-glutamate. In our model, these four amino acids bind with the atoms they share in common (the "main chain" +NH3-CH-COO-) in the same positions. Thus on the basis of our x-ray work, glycine, alanine, and serine appear to inhibit GS-Mn by competing with the substrate glutamate for the active site.
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{{ABSTRACT_PUBMED_8099447}}
==About this Structure==
==About this Structure==
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[[Category: Eisenberg, D.]]
[[Category: Eisenberg, D.]]
[[Category: Liaw, S H.]]
[[Category: Liaw, S H.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:30:16 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:30:09 2008''

Revision as of 06:30, 28 July 2008

Image:2lgs.png

Template:STRUCTURE 2lgs

FEEDBACK INHIBITION OF FULLY UNADENYLYLATED GLUTAMINE SYNTHETASE FROM SALMONELLA TYPHIMURIUM BY GLYCINE, ALANINE, AND SERINE

Template:ABSTRACT PUBMED 8099447

About this Structure

2LGS is a Single protein structure of sequence from Salmonella typhimurium. Full crystallographic information is available from OCA.

Reference

Feedback inhibition of fully unadenylylated glutamine synthetase from Salmonella typhimurium by glycine, alanine, and serine., Liaw SH, Pan C, Eisenberg D, Proc Natl Acad Sci U S A. 1993 Jun 1;90(11):4996-5000. PMID:8099447

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