4bii: Difference between revisions

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New page: '''Unreleased structure''' The entry 4bii is ON HOLD Authors: Read, J.A., Gingell, H. Description: How nature bridges the gap: Crystallographic elucidation of pyridomycin binding to In...
 
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'''Unreleased structure'''


The entry 4bii is ON HOLD
==How nature bridges the gap: Crystallographic elucidation of pyridomycin binding to InhA==
<StructureSection load='4bii' size='340' side='right'caption='[[4bii]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4bii]] is a 4 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=4BII OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BII 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]] 1.95&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <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=4bii FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bii OCA], [https://pdbe.org/4bii PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bii RCSB], [https://www.ebi.ac.uk/pdbsum/4bii PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bii 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.


Authors: Read, J.A., Gingell, H.
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>


Description: How nature bridges the gap: Crystallographic elucidation of pyridomycin binding to InhA
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4bii" 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: Gingell H]]
[[Category: Read JA]]
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