2lgs: Difference between revisions

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[[Image:2lgs.~~jpg~~|left|200px]]

[[Image:2lgs.png|left|200px]]

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

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

~~==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.~~

The line below this paragraph, {{ABSTRACT_PUBMED_8099447}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 8099447 is the PubMed ID number.

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==About this Structure==

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[[Category: Eisenberg, D.]]

[[Category: Liaw, S H.]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May 4~~ 09:30:16 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:30:09 2008''

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-[[Image:2lgs.jpg|left|200px]]
+{{Seed}}
+[[Image:2lgs.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2lgs|  PDB=2lgs  |  SCENE=  }}
-'''FEEDBACK INHIBITION OF FULLY UNADENYLYLATED GLUTAMINE SYNTHETASE FROM SALMONELLA TYPHIMURIUM BY GLYCINE, ALANINE, AND SERINE'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_8099447}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8099447 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_8099447}}
 ==About this Structure==
@@ Line 25: / Line 29: @@
 [[Category: Eisenberg, D.]]
 [[Category: Liaw, S H.]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 09:30:16 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:30:09 2008''