2fr0

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{{STRUCTURE_2fr0| PDB=2fr0 | SCENE= }}
{{STRUCTURE_2fr0| PDB=2fr0 | SCENE= }}
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'''The first ketoreductase of the erythromycin synthase (crystal form 1)'''
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===The first ketoreductase of the erythromycin synthase (crystal form 1)===
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==Overview==
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The structure of the ketoreductase (KR) from the first module of the erythromycin synthase with NADPH bound was solved to 1.79 A resolution. The 51 kDa domain has two subdomains, each similar to a short-chain dehydrogenase/reductase (SDR) monomer. One subdomain has a truncated Rossmann fold and serves a purely structural role stabilizing the other subdomain, which catalyzes the reduction of the beta-carbonyl of a polyketide and possibly the epimerization of an alpha-substituent. The structure enabled us to define the domain boundaries of KR, the dehydratase (DH), and the enoylreductase (ER). It also constrains the three-dimensional organization of these domains within a module, revealing that KR does not make dimeric contacts across the 2-fold axis of the module. The quaternary structure elucidates how substrates are shuttled between the active sites of polyketide synthases (PKSs), as well as related fatty acid synthases (FASs), and suggests how domains can be swapped to make hybrid synthases that produce novel polyketides.
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(as it appears on PubMed at http://www.pubmed.gov), where 16564177 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16564177}}
==About this Structure==
==About this Structure==
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[[Category: Stroud, R M.]]
[[Category: Stroud, R M.]]
[[Category: Short chain dehydrogenase/reductase]]
[[Category: Short chain dehydrogenase/reductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:12:51 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:22:03 2008''

Revision as of 18:22, 27 July 2008

Image:2fr0.png

Template:STRUCTURE 2fr0

The first ketoreductase of the erythromycin synthase (crystal form 1)

Template:ABSTRACT PUBMED 16564177

About this Structure

2FR0 is a Single protein structure of sequence from Saccharopolyspora erythraea. Full crystallographic information is available from OCA.

Reference

The structure of a ketoreductase determines the organization of the beta-carbon processing enzymes of modular polyketide synthases., Keatinge-Clay AT, Stroud RM, Structure. 2006 Apr;14(4):737-48. Epub 2006 Mar 23. PMID:16564177

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