4bii: Difference between revisions
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== | ==How nature bridges the gap: Crystallographic elucidation of pyridomycin binding to InhA== | ||
[[4bii]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <StructureSection load='4bii' size='340' side='right' caption='[[4bii]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4bii]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BII OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BII FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=PYW:PYRIDOMYCIN'>PYW</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4bge|4bge]]</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Enoyl-[acyl-carrier-protein]_reductase_(NADH) Enoyl-[acyl-carrier-protein] reductase (NADH)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.9 1.3.1.9] </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=4bii FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bii OCA], [http://pdbe.org/4bii PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4bii RCSB], [http://www.ebi.ac.uk/pdbsum/4bii PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4bii ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Pyridomycin, a natural product with potent antituberculosis activity, inhibits a major drug target, the InhA enoyl reductase. Here, we unveil the co-crystal structure and unique ability of pyridomycin to block both the NADH cofactor- and lipid substrate-binding pockets of InhA. This is to our knowledge a first-of-a-kind binding mode that discloses a new means of InhA inhibition. Proof-of-principle studies show how structure-assisted drug design can improve the activity of new pyridomycin derivatives. | |||
Pyridomycin bridges the NADH- and substrate-binding pockets of the enoyl reductase InhA.,Hartkoorn RC, Pojer F, Read JA, Gingell H, Neres J, Horlacher OP, Altmann KH, Cole ST Nat Chem Biol. 2013 Dec 1. doi: 10.1038/nchembio.1405. PMID:24292073<ref>PMID:24292073</ref> | |||
<ref | |||
[[Category: | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
[[Category: Gingell, H | </div> | ||
[[Category: Read, J A | <div class="pdbe-citations 4bii" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Enoyl-Acyl-Carrier Protein Reductase|Enoyl-Acyl-Carrier Protein Reductase]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Myctu]] | |||
[[Category: Gingell, H]] | |||
[[Category: Read, J A]] | |||
[[Category: Acp enoyl reductase]] | [[Category: Acp enoyl reductase]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
