1rjm
From Proteopedia
(Difference between revisions)
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<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 [ | + | <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> |
</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='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='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='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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MenB ([ | + | <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'>[ | + | <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'>[ | + | <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> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1rjm ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1rjm ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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. | ||
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| + | 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<ref>PMID:16131752</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 1rjm" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 09:01, 21 July 2021
Crystal Structure of MenB (Rv0548c) from Mycobacterium tuberculosis
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