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1or5

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{{STRUCTURE_1or5| PDB=1or5 | SCENE= }}
{{STRUCTURE_1or5| PDB=1or5 | SCENE= }}
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'''SOLUTION STRUCTURE OF THE HOLO-FORM OF THE FRENOLICIN ACYL CARRIER PROTEIN, MINIMIZED MEAN STRUCTURE'''
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===SOLUTION STRUCTURE OF THE HOLO-FORM OF THE FRENOLICIN ACYL CARRIER PROTEIN, MINIMIZED MEAN STRUCTURE===
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==Overview==
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During polyketide biosynthesis, acyl carrier proteins (ACPs) perform the central role of transferring polyketide intermediates between active sites of polyketide synthase. The 4'-phosphopantetheine prosthetic group of a holo-ACP is a long and flexible arm that can reach into different active sites and provide a terminal sulfhydryl group for the attachment of acyl groups through a thioester linkage. We have determined the solution structure and characterized backbone dynamics of the holo form of the frenolicin acyl carrier protein (fren holo-ACP) by nuclear magnetic resonance (NMR). Unambiguous assignments were made for 433 hydrogen atoms, 333 carbon atoms, and 84 nitrogen atoms, representing a total of 94.6% of the assignable atoms in this protein. From 879 meaningful NOEs and 45 angle constraints, a family of 24 structures has been calculated. The solution structure is composed of three major alpha-helices packed in a bundle with three additional short helices in intervening loops; one of the short helices slowly exchanges between two conformations. Superposition of the major helical regions on the mean structure yields average atomic rmsd values of 0.49 +/- 0.09 and 0.91 +/- 0.08 A for backbone and non-hydrogen atoms, respectively. Although the three-helix bundle fold is conserved among acyl carrier proteins involved in fatty acid synthases and polyketide synthases, a detailed comparison revealed that ACPs from polyketide biosynthetic pathways are more related to each other in tertiary fold than to their homologues from fatty acid biosynthetic pathways. Comparison of the free form of ACPs (NMR structures of fren ACP and the Bacillus subtilis ACP) with the substrate-bound form of ACP (crystal structure of butyryl-ACP from Escherichia coli) suggests that conformational exchange plays a role in substrate binding.
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{{ABSTRACT_PUBMED_12705828}}
==About this Structure==
==About this Structure==
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1OR5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_roseofulvus Streptomyces roseofulvus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OR5 OCA].
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1OR5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_roseofulvus Streptomyces roseofulvus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OR5 OCA].
==Reference==
==Reference==
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[[Category: Pk]]
[[Category: Pk]]
[[Category: Polyketide synthase]]
[[Category: Polyketide synthase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:11:06 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 11:37:18 2008''

Revision as of 08:37, 29 July 2008

Image:1or5.png

Template:STRUCTURE 1or5

SOLUTION STRUCTURE OF THE HOLO-FORM OF THE FRENOLICIN ACYL CARRIER PROTEIN, MINIMIZED MEAN STRUCTURE

Template:ABSTRACT PUBMED 12705828

About this Structure

1OR5 is a Single protein structure of sequence from Streptomyces roseofulvus. Full experimental information is available from OCA.

Reference

Solution structure and backbone dynamics of the holo form of the frenolicin acyl carrier protein., Li Q, Khosla C, Puglisi JD, Liu CW, Biochemistry. 2003 Apr 29;42(16):4648-57. PMID:12705828

Page seeded by OCA on Tue Jul 29 11:37:18 2008

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