2r0g
From Proteopedia
(Difference between revisions)
(New page: 200px<br /><applet load="2r0g" size="350" color="white" frame="true" align="right" spinBox="true" caption="2r0g, resolution 2.37Å" /> '''Chromopyrrolic acid-...) |
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- | [[Image:2r0g.jpg|left|200px]]<br /><applet load="2r0g" size="350" color="white" frame="true" align="right" spinBox="true" | ||
- | caption="2r0g, resolution 2.37Å" /> | ||
- | '''Chromopyrrolic acid-soaked RebC with bound 7-carboxy-K252c'''<br /> | ||
- | == | + | ==Chromopyrrolic acid-soaked RebC with bound 7-carboxy-K252c== |
- | The biosynthesis of rebeccamycin, an antitumor compound, involves the | + | <StructureSection load='2r0g' size='340' side='right'caption='[[2r0g]], [[Resolution|resolution]] 2.37Å' scene=''> |
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[2r0g]] 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=2R0G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2R0G FirstGlance]. <br> | ||
+ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.37Å</td></tr> | ||
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=7CK:7-CARBOXY-5-HYDROXY-12,13-DIHYDRO-6H-INDOLO[2,3-A]PYRROLO[3,4-C]CARBAZOLE'>7CK</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></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=2r0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r0g OCA], [https://pdbe.org/2r0g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2r0g RCSB], [https://www.ebi.ac.uk/pdbsum/2r0g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2r0g ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/Q8KI25_LENAE Q8KI25_LENAE] | ||
+ | == 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/r0/2r0g_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/main_output.php?pdb_ID=2r0g ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The biosynthesis of rebeccamycin, an antitumor compound, involves the remarkable eight-electron oxidation of chlorinated chromopyrrolic acid. Although one rebeccamycin biosynthetic enzyme is capable of generating low levels of the eight-electron oxidation product on its own, a second protein, RebC, is required to accelerate product formation and eliminate side reactions. However, the mode of action of RebC was largely unknown. Using crystallography, we have determined a likely function for RebC as a flavin hydroxylase, captured two snapshots of its dynamic catalytic cycle, and trapped a reactive molecule, a putative substrate, in its binding pocket. These studies strongly suggest that the role of RebC is to sequester a reactive intermediate produced by its partner protein and to react with it enzymatically, preventing its conversion to a suite of degradation products that includes, at low levels, the desired product. | ||
- | + | Crystallographic trapping in the rebeccamycin biosynthetic enzyme RebC.,Ryan KS, Howard-Jones AR, Hamill MJ, Elliott SJ, Walsh CT, Drennan CL Proc Natl Acad Sci U S A. 2007 Sep 25;104(39):15311-6. Epub 2007 Sep 14. PMID:17873060<ref>PMID:17873060</ref> | |
- | + | ||
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | <div class="pdbe-citations 2r0g" style="background-color:#fffaf0;"></div> | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
- | [[Category: | + | [[Category: Large Structures]] |
- | [[Category: | + | [[Category: Lentzea aerocolonigenes]] |
- | [[Category: | + | [[Category: Drennan CL]] |
- | [[Category: | + | [[Category: Ryan KS]] |
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Current revision
Chromopyrrolic acid-soaked RebC with bound 7-carboxy-K252c
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