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| | ==Crystal Structure of type II MenB from Mycobacteria tuberculosis== | | ==Crystal Structure of type II MenB from Mycobacteria tuberculosis== |
| - | <StructureSection load='4qii' size='340' side='right' caption='[[4qii]], [[Resolution|resolution]] 1.64Å' scene=''> | + | <StructureSection load='4qii' size='340' side='right'caption='[[4qii]], [[Resolution|resolution]] 1.64Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4qii]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QII OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QII FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4qii]] 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=4QII OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QII FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2NE:SALICYLYL+COA'>2NE</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.64Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4qij|4qij]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2NE:SALICYLYL+COA'>2NE</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/1,4-dihydroxy-2-naphthoyl-CoA_synthase 1,4-dihydroxy-2-naphthoyl-CoA synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.3.36 4.1.3.36] </span></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=4qii FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qii OCA], [https://pdbe.org/4qii PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qii RCSB], [https://www.ebi.ac.uk/pdbsum/4qii PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qii ProSAT]</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=4qii FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qii OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qii RCSB], [http://www.ebi.ac.uk/pdbsum/4qii PDBsum]</span></td></tr> | + | |
| | </table> | | </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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 4qii" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: 1,4-dihydroxy-2-naphthoyl-CoA synthase]] | + | [[Category: Large Structures]] |
| - | [[Category: Guo, Z H]] | + | [[Category: Mycobacterium tuberculosis H37Rv]] |
| - | [[Category: Song, H G]] | + | [[Category: Guo ZH]] |
| - | [[Category: Sung, H P]] | + | [[Category: Song HG]] |
| - | [[Category: Tse, Y S]] | + | [[Category: Sung HP]] |
| - | [[Category: 4-dihydroxy-2-naphthoyl-coenzyme some]] | + | [[Category: Tse YS]] |
| - | [[Category: Lyase]]
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| - | [[Category: Synthase]]
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| Structural highlights
Function
MENB_MYCTU Converts o-succinylbenzoyl-CoA (OSB-CoA) to 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA).[1]
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Truglio JJ, Theis K, Feng Y, Gajda R, Machutta C, Tonge PJ, Kisker C. Crystal structure of Mycobacterium tuberculosis MenB, a key enzyme in vitamin K2 biosynthesis. J Biol Chem. 2003 Oct 24;278(43):42352-60. Epub 2003 Aug 8. PMID:12909628 doi:http://dx.doi.org/10.1074/jbc.M307399200
- ↑ Song H, Sung HP, Tse YS, Jiang M, Guo Z. Ligand-dependent active-site closure revealed in the crystal structure of Mycobacterium tuberculosis MenB complexed with product analogues. Acta Crystallogr D Biol Crystallogr. 2014 Nov;70(Pt 11):2959-69. doi:, 10.1107/S1399004714019440. Epub 2014 Oct 23. PMID:25372686 doi:http://dx.doi.org/10.1107/S1399004714019440
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