1tqy
From Proteopedia
(New page: 200px<br /><applet load="1tqy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tqy, resolution 2.00Å" /> '''The Actinorhodin Ket...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1tqy.gif|left|200px]]<br /><applet load="1tqy" size=" | + | [[Image:1tqy.gif|left|200px]]<br /><applet load="1tqy" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1tqy, resolution 2.00Å" /> | caption="1tqy, resolution 2.00Å" /> | ||
'''The Actinorhodin Ketosynthase/Chain Length Factor'''<br /> | '''The Actinorhodin Ketosynthase/Chain Length Factor'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The synthesis of aromatic polyketides, such as actinorhodin, tetracycline | + | The synthesis of aromatic polyketides, such as actinorhodin, tetracycline and doxorubicin, begins with the formation of a polyketide chain. In type II polyketide synthases (PKSs), chains are polymerized by the heterodimeric ketosynthase-chain length factor (KS-CLF). Here we present the 2.0-A structure of the actinorhodin KS-CLF, which shows polyketides being elongated inside an amphipathic tunnel approximately 17 A in length at the heterodimer interface. The structure resolves many of the questions about the roles of KS and CLF. Although CLF regulates chain length, it does not have an active site; KS must catalyze both chain initiation and elongation. We provide evidence that the first cyclization of the polyketide occurs within the KS-CLF tunnel. The mechanistic details of this central PKS polymerase could guide biosynthetic chemists in designing new pharmaceuticals and polymers. |
==About this Structure== | ==About this Structure== | ||
| - | 1TQY is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bacteria Bacteria] and [http://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor] with NA, MG and ACE as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Beta-ketoacyl-acyl-carrier-protein_synthase_I Beta-ketoacyl-acyl-carrier-protein synthase I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.41 2.3.1.41] Full crystallographic information is available from [http:// | + | 1TQY is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bacteria Bacteria] and [http://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor] with <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=ACE:'>ACE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Beta-ketoacyl-acyl-carrier-protein_synthase_I Beta-ketoacyl-acyl-carrier-protein synthase I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.41 2.3.1.41] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TQY OCA]. |
==Reference== | ==Reference== | ||
| Line 15: | Line 15: | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Streptomyces coelicolor]] | [[Category: Streptomyces coelicolor]] | ||
| - | [[Category: Keatinge-Clay, A | + | [[Category: Keatinge-Clay, A T.]] |
[[Category: Khosla, C.]] | [[Category: Khosla, C.]] | ||
| - | [[Category: Maltby, D | + | [[Category: Maltby, D A.]] |
| - | [[Category: Medzihradszky, K | + | [[Category: Medzihradszky, K F.]] |
| - | [[Category: Stroud, R | + | [[Category: Stroud, R M.]] |
[[Category: ACE]] | [[Category: ACE]] | ||
[[Category: MG]] | [[Category: MG]] | ||
| Line 26: | Line 26: | ||
[[Category: heterodimer]] | [[Category: heterodimer]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:16:26 2008'' |
Revision as of 13:16, 21 February 2008
|
The Actinorhodin Ketosynthase/Chain Length Factor
Overview
The synthesis of aromatic polyketides, such as actinorhodin, tetracycline and doxorubicin, begins with the formation of a polyketide chain. In type II polyketide synthases (PKSs), chains are polymerized by the heterodimeric ketosynthase-chain length factor (KS-CLF). Here we present the 2.0-A structure of the actinorhodin KS-CLF, which shows polyketides being elongated inside an amphipathic tunnel approximately 17 A in length at the heterodimer interface. The structure resolves many of the questions about the roles of KS and CLF. Although CLF regulates chain length, it does not have an active site; KS must catalyze both chain initiation and elongation. We provide evidence that the first cyclization of the polyketide occurs within the KS-CLF tunnel. The mechanistic details of this central PKS polymerase could guide biosynthetic chemists in designing new pharmaceuticals and polymers.
About this Structure
1TQY is a Protein complex structure of sequences from Bacteria and Streptomyces coelicolor with , and as ligands. Active as Beta-ketoacyl-acyl-carrier-protein synthase I, with EC number 2.3.1.41 Full crystallographic information is available from OCA.
Reference
An antibiotic factory caught in action., Keatinge-Clay AT, Maltby DA, Medzihradszky KF, Khosla C, Stroud RM, Nat Struct Mol Biol. 2004 Sep;11(9):888-93. Epub 2004 Aug 1. PMID:15286722
Page seeded by OCA on Thu Feb 21 15:16:26 2008
