Crystal structures of acyl carrier protein in complex with two catalytic partners show a dynamic role in cellular metabolism.
ACP captured in action: Two recently reported crystal structures are the first to capture ACP-mediated substrate delivery to a catalytic partner at high resolution. These studies highlight key interactions of transient ACP-partner complexes and define the dynamic movements of ACP that facilitate substrate delivery and trigger complex dissociation.
Life Sciences Institute, University of Michigan, 210 Washtenaw Avenue, Ann Arbor, MI 48109 (USA).
Sean A
SA
Newmister
David H
DH
Sherman
D000213:Acyl Carrier Protein / Q000737:chemistry* / Q000378:metabolism*; D000217:Acyltransferases / Q000737:chemistry / Q000378:metabolism*; D055162:Biocatalysis; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000737:chemistry / Q000166:cytology* / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism*; D054889:Fatty Acid Synthase, Type II / Q000737:chemistry* / Q000378:metabolism*; D006836:Hydro-Lyases / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D011485:Protein Binding
D000213:Acyl Carrier Protein; D029968:Escherichia coli Proteins; C040157:acpP protein, E coli; D000217:Acyltransferases; C050304:acyl-(acyl-carrier-protein)-UDP-N-acetylglucosamine acyltransferase; D006836:Hydro-Lyases; C047118:3-hydroxyacyl-(acyl-carrier-protein) dehydratase; D054889:Fatty Acid Synthase, Type II
acyl carrier proteins; biosynthesis; fatty acids; lipid A