3fla
From Proteopedia
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- | [[ | + | ==RifR - Type II thioesterase from Rifamycin NRPS/PKS biosynthetic pathway - Form 1== |
+ | <StructureSection load='3fla' size='340' side='right' caption='[[3fla]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[3fla]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Amycolatopsis_mediterranei Amycolatopsis mediterranei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FLA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FLA FirstGlance]. <br> | ||
+ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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">[[3flb|3flb]]</td></tr> | ||
+ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rifR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=33910 Amycolatopsis mediterranei])</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=3fla FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fla OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3fla RCSB], [http://www.ebi.ac.uk/pdbsum/3fla 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/fl/3fla_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 == | ||
+ | Two thioesterases are commonly found in natural product biosynthetic clusters, a type I thioesterase (TEI) which is responsible for removing the final product from the biosynthetic complex, and a type II thioesterase (TEII) which is believed to perform housekeeping functions such as removing aberrant units from carrier domains. We present the crystal structure and the kinetic analysis of RifR, a TEII from the hybrid NRPS/PKS rifamycin biosynthetic cluster of Amycolatopsis mediterranei. Steady-state kinetics show RifR has a preference for the hydrolysis of acyl units from the phosphopantetheinyl arm (Ppant) of the acyl carrier domain, over the hydrolysis of acyl units from the Ppant of acyl-CoAs as well as a modest preference for the decarboxylated substrate mimics acetyl-CoA and propionyl-CoA over malonyl-CoA and methylmalonyl-CoA. Multiple RifR conformations and structural similarities to other thioesterases suggest that movement of a helical lid controls access of substrates to the active site of RifR. | ||
- | + | Structure and functional analysis of RifR, the type II thioesterase from the rifamycin biosynthetic pathway.,Claxton HB, Akey DL, Silver MK, Admiraal SJ, Smith JL J Biol Chem. 2008 Dec 22. PMID:19103602<ref>PMID:19103602</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
- | + | ||
- | == | + | |
- | < | + | |
[[Category: Amycolatopsis mediterranei]] | [[Category: Amycolatopsis mediterranei]] | ||
- | [[Category: Akey, D L | + | [[Category: Akey, D L]] |
- | [[Category: Smith, J L | + | [[Category: Smith, J L]] |
[[Category: Alpha-beta hydrolase thioesterase]] | [[Category: Alpha-beta hydrolase thioesterase]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] |
Revision as of 10:23, 3 December 2014
RifR - Type II thioesterase from Rifamycin NRPS/PKS biosynthetic pathway - Form 1
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