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4u5q

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<StructureSection load='4u5q' size='340' side='right'caption='[[4u5q]], [[Resolution|resolution]] 1.81&Aring;' scene=''>
<StructureSection load='4u5q' size='340' side='right'caption='[[4u5q]], [[Resolution|resolution]] 1.81&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4u5q]] is a 2 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=4U5Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4U5Q FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4u5q]] is a 2 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=4U5Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4U5Q FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=XPE:3,6,9,12,15,18,21,24,27-NONAOXANONACOSANE-1,29-DIOL'>XPE</scene></td></tr>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=XPE:3,6,9,12,15,18,21,24,27-NONAOXANONACOSANE-1,29-DIOL'>XPE</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4dqv|4dqv]]</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4u5q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u5q OCA], [https://pdbe.org/4u5q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4u5q RCSB], [https://www.ebi.ac.uk/pdbsum/4u5q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4u5q ProSAT]</span></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nrp, Rv0101, LH57_00575 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU])</td></tr>
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<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=4u5q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u5q OCA], [http://pdbe.org/4u5q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4u5q RCSB], [http://www.ebi.ac.uk/pdbsum/4u5q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4u5q ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q10896_MYCTU Q10896_MYCTU]
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In mycobacteria, polyketide synthases and nonribosomal peptide synthetases (NRPSs) produce complex lipidic metabolites by using a thio-template mechanism of catalysis. In this study, we demonstrate that off-loading reductase (R) domain of mycobacterial NRPSs performs two consecutive [2 + 2]e(-) reductions to release thioester-bound lipopeptides as corresponding alcohols, using a nonprocessive mechanism of catalysis. The first crystal structure of an R domain from Mycobacterium tuberculosis NRPS provides strong support to this mechanistic model and suggests that the displacement of intermediate would be required for cofactor recycling. We show that 4e(-) reductases produce alcohols through a committed aldehyde intermediate, and the reduction of this intermediate is at least 10 times more efficient than the thioester-substrate. Structural and biochemical studies also provide evidence for the conformational changes associated with the reductive cycle. Further, we show that the large substrate-binding pocket with a hydrophobic platform accounts for the remarkable substrate promiscuity of these domains. Our studies present an elegant example of the recruitment of a canonical short-chain dehydrogenase/reductase family member as an off-loading domain in the context of assembly-line enzymology.
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Nonprocessive [2 + 2]e- off-loading reductase domains from mycobacterial nonribosomal peptide synthetases.,Chhabra A, Haque AS, Pal RK, Goyal A, Rai R, Joshi S, Panjikar S, Pasha S, Sankaranarayanan R, Gokhale RS Proc Natl Acad Sci U S A. 2012 Apr 10;109(15):5681-6. Epub 2012 Mar 26. PMID:22451903<ref>PMID:22451903</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4u5q" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Myctu]]
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[[Category: Mycobacterium tuberculosis H37Rv]]
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[[Category: Haque, A S]]
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[[Category: Haque AS]]
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[[Category: Patel, K D]]
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[[Category: Patel KD]]
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[[Category: Priyadarshan, K]]
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[[Category: Priyadarshan K]]
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[[Category: Sankaranarayanan, R]]
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[[Category: Sankaranarayanan R]]
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[[Category: Ligase]]
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[[Category: Nonribosomal peptide synthetase]]
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[[Category: Oxidoreductase]]
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[[Category: Short-chain dehydrogenase/reductase]]
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Revision as of 08:03, 22 March 2023

High resolution crystal structure of reductase (R) domain of nonribosomal peptide synthetase from Mycobacterium tuberculosis

PDB ID 4u5q

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