|
|
| Line 3: |
Line 3: |
| | <StructureSection load='1rjm' size='340' side='right'caption='[[1rjm]], [[Resolution|resolution]] 2.15Å' scene=''> | | <StructureSection load='1rjm' size='340' side='right'caption='[[1rjm]], [[Resolution|resolution]] 2.15Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1rjm]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RJM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RJM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1rjm]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RJM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RJM FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EP1:3-[4-(2-HYDROXYETHYL)PIPERAZIN-1-YL]PROPANE-1-SULFONIC+ACID'>EP1</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]] 2.15Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1rjn|1rjn]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EP1:3-[4-(2-HYDROXYETHYL)PIPERAZIN-1-YL]PROPANE-1-SULFONIC+ACID'>EP1</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MenB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</td></tr> | + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/1,4-dihydroxy-2-naphthoyl-CoA_synthase 1,4-dihydroxy-2-naphthoyl-CoA synthase], with EC number [https://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=1rjm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rjm OCA], [https://pdbe.org/1rjm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rjm RCSB], [https://www.ebi.ac.uk/pdbsum/1rjm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rjm ProSAT]</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=1rjm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rjm OCA], [https://pdbe.org/1rjm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rjm RCSB], [https://www.ebi.ac.uk/pdbsum/1rjm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rjm ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == 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>
| + | [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> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 35: |
Line 33: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: 1,4-dihydroxy-2-naphthoyl-CoA synthase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Arcus, V L]] | + | [[Category: Mycobacterium tuberculosis]] |
| - | [[Category: Baker, E N]] | + | [[Category: Arcus VL]] |
| - | [[Category: Johnston, J M]] | + | [[Category: Baker EN]] |
| - | [[Category: Structural genomic]] | + | [[Category: Johnston JM]] |
| - | [[Category: Beta-beta-alpha]]
| + | |
| - | [[Category: Crotonase-like family]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: PSI, Protein structure initiative]]
| + | |
| - | [[Category: Tbsgc]]
| + | |
| Structural highlights
Function
MENB_MYCTU Converts o-succinylbenzoyl-CoA (OSB-CoA) to 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA).[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Mycobacterium tuberculosis, the cause of tuberculosis, is one of the most devastating human pathogens. New drugs for its control are urgently needed. Menaquinone, also known as vitamin K, is an essential cofactor that is required for electron transfer and the enzymes that synthesize it are therefore potential drug targets. The enzyme naphthoate synthase (MenB) from M. tuberculosis has been expressed in Escherichia coli, purified and crystallized both as the native enzyme and in complex with naphthoyl-CoA. Both structures have been determined by X-ray crystallography: native MenB at 2.15 A resolution (R = 0.203, R(free) = 0.231) and its napthoyl-CoA complex at 2.30 A resolution (R = 0.197, R(free) = 0.225). The protein structure, which has a fold characteristic of the crotonase family of enzymes, is notable for the presence of several highly flexible regions around the active site. The bound naphthoyl-CoA is only visible for one of the three molecules in the asymmetric unit and only partly rigidifies the structure. The C-terminal region of the protein is seen to play a critical role both in completion of the binding pocket and in stabilization of the hexamer, suggesting a link between oligomerization and catalytic activity.
Structure of naphthoate synthase (MenB) from Mycobacterium tuberculosis in both native and product-bound forms.,Johnston JM, Arcus VL, Baker EN Acta Crystallogr D Biol Crystallogr. 2005 Sep;61(Pt 9):1199-206. Epub 2005, Aug 16. PMID:16131752[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
- ↑ Johnston JM, Arcus VL, Baker EN. Structure of naphthoate synthase (MenB) from Mycobacterium tuberculosis in both native and product-bound forms. Acta Crystallogr D Biol Crystallogr. 2005 Sep;61(Pt 9):1199-206. Epub 2005, Aug 16. PMID:16131752 doi:http://dx.doi.org/10.1107/S0907444905017531
|
