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2lgs

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Revision as of 07:51, 9 February 2022

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

Structural highlights

2lgs is a 12 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Activity:	Glutamate--ammonia ligase, with EC number 6.3.1.2
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

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

1 Structural highlights
2 Evolutionary Conservation
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2lgs"

Categories: Glutamate--ammonia ligase | Large Structures | Eisenberg, D | Liaw, S H

@@ Line 3: / Line 3: @@
 <StructureSection load='2lgs' size='340' side='right'caption='[[2lgs]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2lgs]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LGS OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2LGS FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2lgs]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LGS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LGS FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glutamate--ammonia_ligase Glutamate--ammonia ligase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.1.2 6.3.1.2] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2lgs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lgs OCA], [http://pdbe.org/2lgs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2lgs RCSB], [http://www.ebi.ac.uk/pdbsum/2lgs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2lgs ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2lgs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lgs OCA], [https://pdbe.org/2lgs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lgs RCSB], [https://www.ebi.ac.uk/pdbsum/2lgs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lgs ProSAT]</span></td></tr>
 </table>
 == Evolutionary Conservation ==

2lgs

From Proteopedia

Revision as of 07:51, 9 February 2022

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

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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