2lgs
From Proteopedia
(New page: 200px<br /><applet load="2lgs" size="450" color="white" frame="true" align="right" spinBox="true" caption="2lgs, resolution 2.8Å" /> '''FEEDBACK INHIBITION O...) |
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| - | [[Image:2lgs.jpg|left|200px]]<br /><applet load="2lgs" size=" | + | [[Image:2lgs.jpg|left|200px]]<br /><applet load="2lgs" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2lgs, resolution 2.8Å" /> | caption="2lgs, resolution 2.8Å" /> | ||
'''FEEDBACK INHIBITION OF FULLY UNADENYLYLATED GLUTAMINE SYNTHETASE FROM SALMONELLA TYPHIMURIUM BY GLYCINE, ALANINE, AND SERINE'''<br /> | '''FEEDBACK INHIBITION OF FULLY UNADENYLYLATED GLUTAMINE SYNTHETASE FROM SALMONELLA TYPHIMURIUM BY GLYCINE, ALANINE, AND SERINE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Bacterial glutamine synthetase (GS; EC 6.3.1.2) was previously shown to be | + | 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== | ==About this Structure== | ||
| - | 2LGS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium] with MN and GLU as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Glutamate--ammonia_ligase Glutamate--ammonia ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.1.2 6.3.1.2] Full crystallographic information is available from [http:// | + | 2LGS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium] with <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=GLU:'>GLU</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Glutamate--ammonia_ligase Glutamate--ammonia ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.1.2 6.3.1.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LGS OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Eisenberg, D.]] | [[Category: Eisenberg, D.]] | ||
| - | [[Category: Liaw, S | + | [[Category: Liaw, S H.]] |
[[Category: GLU]] | [[Category: GLU]] | ||
[[Category: MN]] | [[Category: MN]] | ||
[[Category: ligase(amide synthetase)]] | [[Category: ligase(amide synthetase)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:07:08 2008'' |
Revision as of 16:07, 21 February 2008
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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 and 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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