1mzj
From Proteopedia
(Difference between revisions)
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<StructureSection load='1mzj' size='340' side='right'caption='[[1mzj]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='1mzj' size='340' side='right'caption='[[1mzj]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1mzj]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1mzj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp._R1128 Streptomyces sp. R1128]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MZJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MZJ 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]] 2.1Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene></td></tr> | |
| - | <tr id=' | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mzj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mzj OCA], [https://pdbe.org/1mzj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mzj RCSB], [https://www.ebi.ac.uk/pdbsum/1mzj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mzj ProSAT]</span></td></tr> |
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| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/FABH_STRLI FABH_STRLI] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Has some substrate preference for butyryl-CoA and can tolerate branched substrates. Can also prime acyl-CoA. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids. Involved in the biosynthesis of R1128 polyketide.<ref>PMID:11732905</ref> |
== 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=1mzj 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=1mzj ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | ZhuH is a priming ketosynthase that initiates the elongation of the polyketide chain in the biosynthetic pathway of a type II polyketide, R1128. The crystal structure of ZhuH in complex with the priming substrate acetyl-CoA reveals an extensive loop region at the dimer interface that appears to affect the selectivity for the primer unit. Acetyl-CoA is bound in a 20 A-long channel, which placed the acetyl group against the catalytic triad. Analysis of the primer unit binding site in ZhuH suggests that it can accommodate acyl chains that are two to four carbons long. Selectivity and primer unit size appear to involve the side chains of three residues on the loops close to the dimer interface that constitute the bottom of the substrate binding pocket. | ||
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| - | Crystal structure of the priming beta-ketosynthase from the R1128 polyketide biosynthetic pathway.,Pan H, Tsai S, Meadows ES, Miercke LJ, Keatinge-Clay AT, O'Connell J, Khosla C, Stroud RM Structure. 2002 Nov;10(11):1559-68. PMID:12429097<ref>PMID:12429097</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1mzj" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Streptomyces sp. | + | [[Category: Streptomyces sp. R1128]] |
| - | + | [[Category: Keatinge-Clay A]] | |
| - | [[Category: Keatinge-Clay | + | [[Category: Khosla C]] |
| - | [[Category: Khosla | + | [[Category: Meadows ES]] |
| - | [[Category: Meadows | + | [[Category: Miercke LJW]] |
| - | [[Category: Miercke | + | [[Category: O'Connell J]] |
| - | [[Category: | + | [[Category: Pan H]] |
| - | [[Category: | + | [[Category: Stroud RM]] |
| - | [[Category: | + | [[Category: Tsai SC]] |
| - | [[Category: | + | |
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Revision as of 08:43, 10 April 2024
Crystal Structure of the Priming beta-Ketosynthase from the R1128 Polyketide Biosynthetic Pathway
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