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2hg4

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{{STRUCTURE_2hg4| PDB=2hg4 | SCENE= }}
{{STRUCTURE_2hg4| PDB=2hg4 | SCENE= }}
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'''Structure of the ketosynthase-acyltransferase didomain of module 5 from DEBS.'''
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===Structure of the ketosynthase-acyltransferase didomain of module 5 from DEBS.===
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==Overview==
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The x-ray crystal structure of a 194-kDa fragment from module 5 of the 6-deoxyerythronolide B synthase has been solved at 2.7 Angstrom resolution. Each subunit of the homodimeric protein contains a full-length ketosynthase (KS) and acyl transferase (AT) domain as well as three flanking "linkers." The linkers are structurally well defined and contribute extensively to intersubunit or interdomain interactions, frequently by means of multiple highly conserved residues. The crystal structure also reveals that the active site residue Cys-199 of the KS domain is separated from the active site residue Ser-642 of the AT domain by approximately 80 Angstrom. This distance is too large to be covered simply by alternative positioning of a statically anchored, fully extended phosphopantetheine arm of the acyl carrier protein domain from module 5. Thus, substantial domain reorganization appears necessary for the acyl carrier protein to interact successively with both the AT and the KS domains of this prototypical polyketide synthase module. The 2.7-Angstrom KS-AT structure is fully consistent with a recently reported lower resolution, 4.5-Angstrom model of fatty acid synthase structure, and emphasizes the close biochemical and structural similarity between polyketide synthase and fatty acid synthase enzymology.
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(as it appears on PubMed at http://www.pubmed.gov), where 16844787 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16844787}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
The 2.7-Angstrom crystal structure of a 194-kDa homodimeric fragment of the 6-deoxyerythronolide B synthase., Tang Y, Kim CY, Mathews II, Cane DE, Khosla C, Proc Natl Acad Sci U S A. 2006 Jul 25;103(30):11124-9. Epub 2006 Jul 14. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16844787 16844787]
The 2.7-Angstrom crystal structure of a 194-kDa homodimeric fragment of the 6-deoxyerythronolide B synthase., Tang Y, Kim CY, Mathews II, Cane DE, Khosla C, Proc Natl Acad Sci U S A. 2006 Jul 25;103(30):11124-9. Epub 2006 Jul 14. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16844787 16844787]
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Reconstituting modular activity from separated domains of 6-deoxyerythronolide B synthase., Kim CY, Alekseyev VY, Chen AY, Tang Y, Cane DE, Khosla C, Biochemistry. 2004 Nov 9;43(44):13892-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15518537 15518537]
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Harnessing the biosynthetic code: combinations, permutations, and mutations., Cane DE, Walsh CT, Khosla C, Science. 1998 Oct 2;282(5386):63-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9756477 9756477]
[[Category: Erythronolide synthase]]
[[Category: Erythronolide synthase]]
[[Category: Saccharopolyspora erythraea]]
[[Category: Saccharopolyspora erythraea]]
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[[Category: Ketosynthase]]
[[Category: Ketosynthase]]
[[Category: Module 5]]
[[Category: Module 5]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:15:07 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 22:59:20 2008''

Revision as of 19:59, 27 July 2008

Image:2hg4.png

Template:STRUCTURE 2hg4

Structure of the ketosynthase-acyltransferase didomain of module 5 from DEBS.

Template:ABSTRACT PUBMED 16844787

About this Structure

2HG4 is a Single protein structure of sequence from Saccharopolyspora erythraea. Full crystallographic information is available from OCA.

Reference

The 2.7-Angstrom crystal structure of a 194-kDa homodimeric fragment of the 6-deoxyerythronolide B synthase., Tang Y, Kim CY, Mathews II, Cane DE, Khosla C, Proc Natl Acad Sci U S A. 2006 Jul 25;103(30):11124-9. Epub 2006 Jul 14. PMID:16844787

Reconstituting modular activity from separated domains of 6-deoxyerythronolide B synthase., Kim CY, Alekseyev VY, Chen AY, Tang Y, Cane DE, Khosla C, Biochemistry. 2004 Nov 9;43(44):13892-8. PMID:15518537

Harnessing the biosynthetic code: combinations, permutations, and mutations., Cane DE, Walsh CT, Khosla C, Science. 1998 Oct 2;282(5386):63-8. PMID:9756477

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