3flb
From Proteopedia
(Difference between revisions)
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<StructureSection load='3flb' size='340' side='right'caption='[[3flb]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='3flb' size='340' side='right'caption='[[3flb]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3flb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3flb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Amycolatopsis_mediterranei Amycolatopsis mediterranei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FLB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FLB FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></td></tr> |
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3flb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3flb OCA], [https://pdbe.org/3flb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3flb RCSB], [https://www.ebi.ac.uk/pdbsum/3flb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3flb ProSAT]</span></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=3flb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3flb OCA], [https://pdbe.org/3flb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3flb RCSB], [https://www.ebi.ac.uk/pdbsum/3flb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3flb ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q7BUF9_AMYMD Q7BUF9_AMYMD] | ||
== 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=3flb 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=3flb ConSurf]. | ||
<div style="clear:both"></div> | <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. | ||
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| - | 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> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 3flb" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Amycolatopsis mediterranei]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Akey | + | [[Category: Akey DL]] |
| - | [[Category: Smith | + | [[Category: Smith JL]] |
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Current revision
RifR - Type II thioesterase from Rifamycin NRPS/PKS biosynthetic pathway - Form 2
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