1l0h: Difference between revisions

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-[[Image:1l0h.jpg|left|200px]]
+{{Seed}}
+[[Image:1l0h.png|left|200px]]
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 {{STRUCTURE_1l0h|  PDB=1l0h  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF BUTYRYL-ACP FROM E.COLI'''
+===CRYSTAL STRUCTURE OF BUTYRYL-ACP FROM E.COLI===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12057197}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12057197 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12057197}}
 ==About this Structure==
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 [[Category: Crystal structure]]
 [[Category: Fatty acid biosynthesis]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 23:24:01 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  2 11:25:47 2008''