4bge: Difference between revisions
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New page: '''Unreleased structure''' The entry 4bge is ON HOLD Authors: Pojer, F., Hartkoorn, R.C., Cole, S.T. Description: Crystal structure of InhA(S94A) mutant in complex with pyridomycin |
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==Crystal structure of InhA(S94A) mutant in complex with pyridomycin== | |||
<StructureSection load='4bge' size='340' side='right'caption='[[4bge]], [[Resolution|resolution]] 2.25Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4bge]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BGE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BGE FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PYW:PYRIDOMYCIN'>PYW</scene></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=4bge FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bge OCA], [https://pdbe.org/4bge PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bge RCSB], [https://www.ebi.ac.uk/pdbsum/4bge PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bge ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/INHA_MYCTU INHA_MYCTU] | |||
<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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4bge" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Enoyl-Acyl-Carrier Protein Reductase 3D structures|Enoyl-Acyl-Carrier Protein Reductase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mycobacterium tuberculosis H37Rv]] | |||
[[Category: Cole ST]] | |||
[[Category: Hartkoorn RC]] | |||
[[Category: Pojer F]] | |||
Latest revision as of 14:50, 20 December 2023
Crystal structure of InhA(S94A) mutant in complex with pyridomycinCrystal structure of InhA(S94A) mutant in complex with pyridomycin
Structural highlights
FunctionPublication Abstract from PubMedPyridomycin, 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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