3zoi
From Proteopedia
(Difference between revisions)
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- | + | ==ISOPENICILLIN N SYNTHASE WITH AC-O-METHYL-D-THREONINE== | |
- | === | + | <StructureSection load='3zoi' size='340' side='right' caption='[[3zoi]], [[Resolution|resolution]] 1.82Å' scene=''> |
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[3zoi]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/A._nidulans A. nidulans]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2y86 2y86]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZOI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZOI FirstGlance]. <br> | ||
+ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=M2W:DELTA-(L-ALPHA-AMINOADIPOYL)-L-CYSTEINYL-O-METHYL-D-THREONINE'>M2W</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
+ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Isopenicillin-N_synthase Isopenicillin-N synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.21.3.1 1.21.3.1] </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=3zoi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zoi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3zoi RCSB], [http://www.ebi.ac.uk/pdbsum/3zoi PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Isopenicillin N synthase (IPNS) is a non-heme iron oxidase central to the biosynthesis of beta-lactam antibiotics. IPNS converts the tripeptide delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-valine (ACV) to isopenicillin N while reducing molecular oxygen to water. The substrate analogue delta-(L-alpha-aminoadipoyl)-L-cysteinyl-O-methyl-D-threonine (ACmT) is not turned over by IPNS. Epimeric delta-(L-alpha-aminoadipoyl)-L-cysteinyl-O-methyl-D-allo-threonine (ACmaT) is converted to a bioactive penam product. ACmT and ACmaT differ from each other only in the stereochemistry at the beta-carbon atom of their third residue. These substrates both contain a methyl ether in place of the isopropyl group of ACV. We report an X-ray crystal structure for the anaerobic IPNS:Fe(II):ACmT complex. This structure reveals an additional water molecule bound to the active site metal, held by hydrogen-bonding to the ether oxygen atom of the substrate analogue. | ||
- | + | The crystal structure of an isopenicillin N synthase complex with an ethereal substrate analogue reveals water in the oxygen binding site.,Clifton IJ, Ge W, Adlington RM, Baldwin JE, Rutledge PJ FEBS Lett. 2013 Aug 19;587(16):2705-9. doi: 10.1016/j.febslet.2013.07.016. Epub, 2013 Jul 13. PMID:23860486<ref>PMID:23860486</ref> | |
- | + | ||
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | [[Category: | + | == References == |
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: A. nidulans]] | ||
[[Category: Isopenicillin-N synthase]] | [[Category: Isopenicillin-N synthase]] | ||
[[Category: Clifton, I J.]] | [[Category: Clifton, I J.]] |
Revision as of 08:44, 22 October 2014
ISOPENICILLIN N SYNTHASE WITH AC-O-METHYL-D-THREONINE
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