2d52
From Proteopedia
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|PDB= 2d52 |SIZE=350|CAPTION= <scene name='initialview01'>2d52</scene>, resolution 1.6Å | |PDB= 2d52 |SIZE=350|CAPTION= <scene name='initialview01'>2d52</scene>, resolution 1.6Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=COA:COENZYME A'>COA</scene> | + | |LIGAND= <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2d3m|2D3M]], [[1bq6|1BQ6]], [[1ee0|1EE0]], [[2d51|2D51]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2d52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d52 OCA], [http://www.ebi.ac.uk/pdbsum/2d52 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2d52 RCSB]</span> | ||
}} | }} | ||
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[[Category: Kohno, T.]] | [[Category: Kohno, T.]] | ||
[[Category: Morita, H.]] | [[Category: Morita, H.]] | ||
| - | [[Category: COA]] | ||
[[Category: chalcone synthase]] | [[Category: chalcone synthase]] | ||
[[Category: pentaketide chromone synthase]] | [[Category: pentaketide chromone synthase]] | ||
[[Category: polyketide synthase]] | [[Category: polyketide synthase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:30:23 2008'' |
Revision as of 23:30, 30 March 2008
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| , resolution 1.6Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Related: | 2D3M, 1BQ6, 1EE0, 2D51
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Pentaketide chromone synthase (M207G mutant complexed with Coa)
Overview
The crystal structures of a wild-type and a mutant PCS, a novel plant type III polyketide synthase from a medicinal plant, Aloe arborescens, were solved at 1.6 A resolution. The crystal structures revealed that the pentaketide-producing wild-type and the octaketide-producing M207G mutant shared almost the same overall folding, and that the large-to-small substitution dramatically increases the volume of the polyketide-elongation tunnel by opening a gate to two hidden pockets behind the active site of the enzyme. The chemically inert active site residue 207 thus controls the number of condensations of malonyl-CoA, solely depending on the steric bulk of the side chain. These findings not only provided insight into the polyketide formation reaction, but they also suggested strategies for the engineered biosynthesis of polyketides.
About this Structure
2D52 is a Single protein structure of sequence from Aloe arborescens. Full crystallographic information is available from OCA.
Reference
Structural insight into chain-length control and product specificity of pentaketide chromone synthase from Aloe arborescens., Morita H, Kondo S, Oguro S, Noguchi H, Sugio S, Abe I, Kohno T, Chem Biol. 2007 Apr;14(4):359-69. PMID:17462571
Page seeded by OCA on Mon Mar 31 02:30:23 2008
