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]] 3.50&Aring;' scene=''>
+<StructureSection load='3o6x' size='340' side='right'caption='[[3o6x]], [[Resolution|resolution]] 3.50&Aring;' 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>
+<table><tr><td colspan='2'>[[3o6x]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteroides_fragilis_NCTC_9343 Bacteroides fragilis NCTC 9343]. 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 [https://proteopedia.org/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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.5&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='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>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3o6x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o6x OCA], [https://pdbe.org/3o6x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o6x RCSB], [https://www.ebi.ac.uk/pdbsum/3o6x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o6x ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/Q5LGP1_BACFN Q5LGP1_BACFN]
-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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+==See Also==
-</div>
+*[[Glutamine synthetase 3D structures|Glutamine synthetase 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Bacteroides fragilis]]
+[[Category: Bacteroides fragilis NCTC 9343]]
-[[Category: Abratt, V R]]
+[[Category: Large Structures]]
-[[Category: Belrhali, H]]
+[[Category: Abratt VR]]
-[[Category: Rooyen, J M.van]]
+[[Category: Belrhali H]]
-[[Category: Sewell, B T]]
+[[Category: Sewell BT]]
-[[Category: Beta barrel]]
+[[Category: Van Rooyen JM]]
-[[Category: Dodecamer]]
-[[Category: Glutamine synthetase]]
-[[Category: Ligase]]
-[[Category: Type iii]]