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Structural modification of acyl carrier protein by butyryl group.


ABSTRACT: Fatty acid synthesis in bacteria is catalyzed by a set of individual enzymes known as the type II fatty acid synthase. Acyl carrier protein (ACP) shuttles the acyl intermediates between individual pathway enzymes. In this study, we determined the solution structures of three different forms of ACP, apo-ACP, ACP, and butyryl-ACP under identical experimental conditions. The structural studies revealed that attachment of butyryl acyl intermediate to ACP alters the conformation of ACP. This finding supports the more general notion that the attachment of different acyl intermediates alters the ACP structure to facilitate their recognition and turnover by the appropriate target enzymes.

SUBMITTER: Wu BN 

PROVIDER: S-EPMC2708020 | biostudies-literature | 2009 Jan

REPOSITORIES: biostudies-literature

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Structural modification of acyl carrier protein by butyryl group.

Wu Bai-Nan BN   Zhang Yong-Mei YM   Rock Charles O CO   Zheng Jie J JJ  

Protein science : a publication of the Protein Society 20090101 1


Fatty acid synthesis in bacteria is catalyzed by a set of individual enzymes known as the type II fatty acid synthase. Acyl carrier protein (ACP) shuttles the acyl intermediates between individual pathway enzymes. In this study, we determined the solution structures of three different forms of ACP, apo-ACP, ACP, and butyryl-ACP under identical experimental conditions. The structural studies revealed that attachment of butyryl acyl intermediate to ACP alters the conformation of ACP. This finding  ...[more]

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