6cnz: Difference between revisions
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<StructureSection load='6cnz' size='340' side='right' caption='[[6cnz]], [[Resolution|resolution]] 2.15Å' scene=''> | <StructureSection load='6cnz' size='340' side='right' caption='[[6cnz]], [[Resolution|resolution]] 2.15Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6cnz]] is a 6 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4oj7 4oj7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CNZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CNZ FirstGlance]. <br> | <table><tr><td colspan='2'>[[6cnz]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_700388 Atcc 700388]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4oj7 4oj7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CNZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CNZ FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AQ477_14105, CRX59_12655 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=57975 ATCC 700388])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Chorismate_mutase Chorismate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.5 5.4.99.5] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Chorismate_mutase Chorismate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.5 5.4.99.5] </span></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=6cnz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cnz OCA], [http://pdbe.org/6cnz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cnz RCSB], [http://www.ebi.ac.uk/pdbsum/6cnz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cnz ProSAT]</span></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=6cnz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cnz OCA], [http://pdbe.org/6cnz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cnz RCSB], [http://www.ebi.ac.uk/pdbsum/6cnz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cnz ProSAT]</span></td></tr> | ||
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/A0A1B4JXW9_BURTH A0A1B4JXW9_BURTH]] Catalyzes the Claisen rearrangement of chorismate to prephenate.[PIRNR:PIRNR026640] | [[http://www.uniprot.org/uniprot/A0A1B4JXW9_BURTH A0A1B4JXW9_BURTH]] Catalyzes the Claisen rearrangement of chorismate to prephenate.[PIRNR:PIRNR026640] | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Burkholderia thailandensis is often used as a model for more virulent members of this genus of proteobacteria that are highly antibiotic-resistant and are potential agents of biological warfare that are infective by inhalation. As part of ongoing efforts to identify potential targets for the development of rational therapeutics, the structures of enzymes that are absent in humans, including that of chorismate mutase from B. thailandensis, have been determined by the Seattle Structural Genomics Center for Infectious Disease. The high-resolution structure of chorismate mutase from B. thailandensis was determined in the monoclinic space group P21 with three homodimers per asymmetric unit. The overall structure of each protomer has the prototypical AroQgamma topology and shares conserved binding-cavity residues with other chorismate mutases, including those with which it has no appreciable sequence identity. | |||
Crystal structure of chorismate mutase from Burkholderia thailandensis.,Asojo OA, Dranow DM, Serbzhinskiy D, Subramanian S, Staker B, Edwards TE, Myler PJ Acta Crystallogr F Struct Biol Commun. 2018 May 1;74(Pt 5):294-299. doi:, 10.1107/S2053230X1800506X. Epub 2018 Apr 16. PMID:29717997<ref>PMID:29717997</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6cnz" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Atcc 700388]] | |||
[[Category: Chorismate mutase]] | [[Category: Chorismate mutase]] | ||
[[Category: Structural genomic]] | [[Category: Structural genomic]] | ||
[[Category: Isomerase]] | [[Category: Isomerase]] | ||
[[Category: Ssgcid]] | [[Category: Ssgcid]] | ||