View source for 4qij


==Crystal structure of MenB from Mycobacteria tuberculosis in complex with 1-HNA-CoA==
<StructureSection load='4qij' size='340' side='right'caption='[[4qij]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4qij]] is a 12 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=4QIJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QIJ 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]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1HA:1-HYDROXY-2-NAPHTHOYL-COA'>1HA</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=4qij FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qij OCA], [https://pdbe.org/4qij PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qij RCSB], [https://www.ebi.ac.uk/pdbsum/4qij PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qij ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MENB_MYCTU MENB_MYCTU] Converts o-succinylbenzoyl-CoA (OSB-CoA) to 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA).<ref>PMID:12909628</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
1,4-Dihydroxy-2-naphthoyl coenzyme A (DHNA-CoA) synthase catalyzes an essential intramolecular Claisen condensation in menaquinone biosynthesis and is an important target for the development of new antibiotics. This enzyme in Mycobacterium tuberculosis is cofactor-free and is classified as a type II DHNA-CoA synthase, differing from type I enzymes, which rely on exogenous bicarbonate for catalysis. Its crystal structures in complex with product analogues have been determined at high resolution to reveal ligand-dependent structural changes, which include the ordering of a 27-residue active-site loop (amino acids 107-133) and the reorientation of the carboxy-terminal helix (amino acids 289-301) that forms part of the active site from the opposing subunit across the trimer-trimer interface. These structural changes result in closure of the active site to the bulk solution, which is likely to take place through an induced-fit mechanism, similar to that observed for type I DHNA-CoA synthases. These findings demonstrate that the ligand-dependent conformational changes are a conserved feature of all DHNA-CoA synthases, providing new insights into the catalytic mechanism of this essential tubercular enzyme.

Ligand-dependent active-site closure revealed in the crystal structure of Mycobacterium tuberculosis MenB complexed with product analogues.,Song H, Sung HP, Tse YS, Jiang M, Guo Z Acta Crystallogr D Biol Crystallogr. 2014 Nov;70(Pt 11):2959-69. doi:, 10.1107/S1399004714019440. Epub 2014 Oct 23. PMID:25372686<ref>PMID:25372686</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4qij" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mycobacterium tuberculosis H37Rv]]
[[Category: Guo ZH]]
[[Category: Song HG]]
[[Category: Sung HP]]
[[Category: Tse YS]]