2lgs
From Proteopedia
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FEEDBACK INHIBITION OF FULLY UNADENYLYLATED GLUTAMINE SYNTHETASE FROM SALMONELLA TYPHIMURIUM BY GLYCINE, ALANINE, AND SERINE
Overview
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.
About this Structure
2LGS is a Single protein structure of sequence from Salmonella typhimurium with MN and GLU as ligands. Active as Glutamate--ammonia ligase, with EC number 6.3.1.2 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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