3o6x: Difference between revisions
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==Crystal Structure of the type III Glutamine Synthetase from Bacteroides fragilis== | |||
<StructureSection load='3o6x' size='340' side='right' caption='[[3o6x]], [[Resolution|resolution]] 3.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3o6x]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacteroides_fragilis Bacteroides fragilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O6X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3O6X FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=P3S:L-METHIONINE-S-SULFOXIMINE+PHOSPHATE'>P3S</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BF0955, glnA, GlnN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=817 Bacteroides fragilis])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3o6x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o6x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3o6x RCSB], [http://www.ebi.ac.uk/pdbsum/3o6x PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Glutamine synthetases are ubiquitous, homo-oligomeric enzymes essential for nitrogen metabolism. Unlike types I and II, which are well described both structurally and functionally, the larger, type IIIs are poorly characterized despite their widespread occurrence. An understanding of the structural basis for this divergence and the implications for design of type-specific inhibitors has, therefore, been impossible. The first crystal structure of a GSIII enzyme, presented here, reveals a conservation of the GS catalytic fold but subtle differences in protein-ligand interactions suggest possible avenues for the design GSIII inhibitors. Despite these similarities, the divergence of the GSIII enzymes can be explained by differences in quaternary structure. Unexpectedly, the two hexameric rings of the GSIII dodecamer associate on the opposite surface relative to types I and II. The diversity of GS quaternary structures revealed here suggests a nonallosteric role for the evolution of the double-ringed architecture seen in all GS enzymes. | |||
Crystal Structure of Type III Glutamine Synthetase: Surprising Reversal of the Inter-Ring Interface.,van Rooyen JM, Abratt VR, Belrhali H, Sewell T Structure. 2011 Apr 13;19(4):471-83. PMID:21481771<ref>PMID:21481771</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
< | </div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bacteroides fragilis]] | [[Category: Bacteroides fragilis]] | ||
[[Category: Abratt, V R | [[Category: Abratt, V R]] | ||
[[Category: Belrhali, H | [[Category: Belrhali, H]] | ||
[[Category: Rooyen, J M.van | [[Category: Rooyen, J M.van]] | ||
[[Category: Sewell, B T | [[Category: Sewell, B T]] | ||
[[Category: Beta barrel]] | [[Category: Beta barrel]] | ||
[[Category: Dodecamer]] | [[Category: Dodecamer]] | ||
Revision as of 09:43, 19 December 2014
Crystal Structure of the type III Glutamine Synthetase from Bacteroides fragilisCrystal Structure of the type III Glutamine Synthetase from Bacteroides fragilis
Structural highlights
Publication Abstract from PubMedGlutamine synthetases are ubiquitous, homo-oligomeric enzymes essential for nitrogen metabolism. Unlike types I and II, which are well described both structurally and functionally, the larger, type IIIs are poorly characterized despite their widespread occurrence. An understanding of the structural basis for this divergence and the implications for design of type-specific inhibitors has, therefore, been impossible. The first crystal structure of a GSIII enzyme, presented here, reveals a conservation of the GS catalytic fold but subtle differences in protein-ligand interactions suggest possible avenues for the design GSIII inhibitors. Despite these similarities, the divergence of the GSIII enzymes can be explained by differences in quaternary structure. Unexpectedly, the two hexameric rings of the GSIII dodecamer associate on the opposite surface relative to types I and II. The diversity of GS quaternary structures revealed here suggests a nonallosteric role for the evolution of the double-ringed architecture seen in all GS enzymes. Crystal Structure of Type III Glutamine Synthetase: Surprising Reversal of the Inter-Ring Interface.,van Rooyen JM, Abratt VR, Belrhali H, Sewell T Structure. 2011 Apr 13;19(4):471-83. PMID:21481771[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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