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3gxo
From Proteopedia
(Difference between revisions)
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| - | + | ==Structure of the Mitomycin 7-O-methyltransferase MmcR with bound Mitomycin A== | |
| - | + | <StructureSection load='3gxo' size='340' side='right' caption='[[3gxo]], [[Resolution|resolution]] 2.30Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[3gxo]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_lavendulae Streptomyces lavendulae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GXO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3GXO FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MQA:[(1AS,8S,8AR,8BS)-6,8A-DIMETHOXY-5-METHYL-4,7-DIOXO-1,1A,2,4,7,8,8A,8B-OCTAHYDROAZIRENO[2,3 3,4]PYRROLO[1,2-A]INDOL-8-YL]METHYL+CARBAMATE'>MQA</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3gwz|3gwz]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mmcR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1914 Streptomyces lavendulae])</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=3gxo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gxo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3gxo RCSB], [http://www.ebi.ac.uk/pdbsum/3gxo PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gx/3gxo_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Mitomycins are quinone-containing antibiotics, widely used as antitumor drugs in chemotherapy. Mitomycin-7-O-methyltransferase (MmcR), a key tailoring enzyme involved in the biosynthesis of mitomycin in Streptomyces lavendulae, catalyzes the 7-O-methylation of both C9beta- and C9alpha-configured 7-hydroxymitomycins. We have determined the crystal structures of the MmcR-S-adenosylhomocysteine (SAH) binary complex and MmcR-SAH-mitomycin A (MMA) ternary complex at resolutions of 1.9and 2.3 A, respectively. The study revealed MmcR to adopt a common S-adenosyl-L-methionine-dependent O-methyltransferase fold and the presence of a structurally conserved active site general acid-base pair is consistent with a proton-assisted methyltransfer common to most methyltransferases. Given the importance of C7 alkylation to modulate mitomycin redox potential, this study may also present a template toward the future engineering of catalysts to generate uniquely bioactive mitomycins. Proteins 2011. (c) 2011 Wiley-Liss, Inc. | ||
| - | + | Structural characterization of the mitomycin 7-O-methyltransferase.,Singh S, Chang A, Goff RD, Bingman CA, Gruschow S, Sherman DH, Phillips GN Jr, Thorson JS Proteins. 2011 Mar 22. doi: 10.1002/prot.23040. PMID:21538548<ref>PMID:21538548</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Streptomyces lavendulae]] | [[Category: Streptomyces lavendulae]] | ||
| - | [[Category: Bingman, C A | + | [[Category: Bingman, C A]] |
| - | [[Category: Chang, A | + | [[Category: Chang, A]] |
| - | [[Category: Phillips, G N | + | [[Category: Phillips, G N]] |
| - | [[Category: Singh, S | + | [[Category: Singh, S]] |
| - | [[Category: Thorson, J S | + | [[Category: Thorson, J S]] |
[[Category: Methyltransferase]] | [[Category: Methyltransferase]] | ||
[[Category: Mitomycin]] | [[Category: Mitomycin]] | ||
Revision as of 16:23, 18 December 2014
Structure of the Mitomycin 7-O-methyltransferase MmcR with bound Mitomycin A
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