3bus: Difference between revisions

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-[[Image:3bus.jpg|left|200px]]
-<!--
+==Crystal Structure of RebM==
-The line below this paragraph, containing "STRUCTURE_3bus", creates the "Structure Box" on the page.
+<StructureSection load='3bus' size='340' side='right'caption='[[3bus]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[3bus]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lentzea_aerocolonigenes Lentzea aerocolonigenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BUS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BUS FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.65&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
-{{STRUCTURE_3bus|  PDB=3bus  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3bus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bus OCA], [https://pdbe.org/3bus PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bus RCSB], [https://www.ebi.ac.uk/pdbsum/3bus PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bus ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/REBMT_LENAE REBMT_LENAE] Glycosyl O-methyltransferase that catalyzes the final step in the biosynthesis of rebeccamycin, an indolocarbazole alkaloid that inhibits topoisomerase 1. Has broad substrate specificity and functions as glycosyl O-methyltransferase on a number of rebeccamycin analogs.<ref>PMID:16575939</ref> <ref>PMID:18502766</ref>
+== 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/bu/3bus_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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/main_output.php?pdb_ID=3bus ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The 2.65-angstroms crystal structure of the rebeccamycin 4'-O-methyltransferase RebM in complex with S-adenosyl-l-homocysteine revealed RebM to adopt a typical S-adenosylmethionine-binding fold of small molecule O-methyltransferases (O-MTases) and display a weak dimerization domain unique to MTases. Using this structure as a basis, the RebM substrate binding model implicated a predominance of nonspecific hydrophobic interactions consistent with the reported ability of RebM to methylate a wide range of indolocarbazole surrogates. This model also illuminated the three putative RebM catalytic residues (His140/141 and Asp166) subsequently found to be highly conserved among sequence-related natural product O-MTases from GC-rich bacteria. Interrogation of these residues via site-directed mutagenesis in RebM demonstrated His140 and Asp166 to be most important for catalysis. This study reveals RebM to be a member of the general acid/base-dependent O-MTases and, as the first crystal structure for a sugar O-MTase, may also present a template toward the future engineering of natural product MTases for combinatorial applications.
-'''Crystal Structure of RebM'''
+Structure and mechanism of the rebeccamycin sugar 4'-O-methyltransferase RebM.,Singh S, McCoy JG, Zhang C, Bingman CA, Phillips GN Jr, Thorson JS J Biol Chem. 2008 Aug 15;283(33):22628-36. Epub 2008 May 23. PMID:18502766<ref>PMID:18502766</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-==About this Structure==
+</div>
-BUS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Lechevalieria_aerocolonigenes Lechevalieria aerocolonigenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BUS OCA].
+<div class="pdbe-citations 3bus" style="background-color:#fffaf0;"></div>
-[[Category: Lechevalieria aerocolonigenes]]
+== References ==
-[[Category: Single protein]]
+<references/>
-[[Category: Bingman, C A.]]
+__TOC__
-[[Category: McCoy, J G.]]
+</StructureSection>
-[[Category: Phillips, G N.]]
+[[Category: Large Structures]]
-[[Category: Singh, S.]]
+[[Category: Lentzea aerocolonigenes]]
-[[Category: Thorson, J S.]]
+[[Category: Bingman CA]]
-[[Category: Methyltransferase]]
+[[Category: McCoy JG]]
-[[Category: Rebeccamycin synthesis]]
+[[Category: Phillips Jr GN]]
-[[Category: Transferase]]
+[[Category: Singh S]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 21:07:47 2008''
+[[Category: Thorson JS]]