1l0h

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{{STRUCTURE_1l0h| PDB=1l0h | SCENE= }}
{{STRUCTURE_1l0h| PDB=1l0h | SCENE= }}
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'''CRYSTAL STRUCTURE OF BUTYRYL-ACP FROM E.COLI'''
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===CRYSTAL STRUCTURE OF BUTYRYL-ACP FROM E.COLI===
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==Overview==
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Acyl carrier protein (ACP) is an essential cofactor in biosynthesis of fatty acids and many other reactions that require acyl transfer steps. We have determined the first crystal structures of an acylated form of ACP from E. coli, that of butyryl-ACP. Our analysis of the molecular surface of ACP reveals a plastic hydrophobic cavity in the vicinity of the phosphopantethylated Ser36 residue that is expanded and occupied by the butyryl and beta-mercaptoethylamine moieties of the acylated 4'-phosphopantetheine group in one of our crystal forms. In the other form, the cavity is contracted, and we propose that the protein has adopted the conformation after delivery of substrate into the active site of a partner enzyme.
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(as it appears on PubMed at http://www.pubmed.gov), where 12057197 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12057197}}
==About this Structure==
==About this Structure==
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[[Category: Crystal structure]]
[[Category: Crystal structure]]
[[Category: Fatty acid biosynthesis]]
[[Category: Fatty acid biosynthesis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 11:25:47 2008''

Revision as of 08:25, 2 July 2008

Image:1l0h.png

Template:STRUCTURE 1l0h

CRYSTAL STRUCTURE OF BUTYRYL-ACP FROM E.COLI

Template:ABSTRACT PUBMED 12057197

About this Structure

1L0H is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

X-ray crystallographic studies on butyryl-ACP reveal flexibility of the structure around a putative acyl chain binding site., Roujeinikova A, Baldock C, Simon WJ, Gilroy J, Baker PJ, Stuitje AR, Rice DW, Slabas AR, Rafferty JB, Structure. 2002 Jun;10(6):825-35. PMID:12057197

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