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Literature DB >> 24771327

Crystal structures of acyl carrier protein in complex with two catalytic partners show a dynamic role in cellular metabolism.

Abstract

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.

Entities: Chemical Gene Species

Keywords: acyl carrier proteins; biosynthesis; fatty acids; lipid A

Mesh：

Substances：

Year: 2014 PMID： 24771327 PMCID： PMC4122295 DOI： 10.1002/cbic.201402095

Source DB: PubMed Journal: Chembiochem ISSN： 1439-4227 Impact factor: 3.164

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References

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Crystal structures of acyl carrier protein in complex with two catalytic partners show a dynamic role in cellular metabolism.

Review 1. The structural role of the carrier protein--active controller or passive carrier.

2. Beta-hydroxydecanoyl thioester dehydrase. Studies on molecular structure and active site.

3. On the enzymatic synthesis of unsaturated fatty acids in Escherichia coli.

4. Dehydratase-specific probes for fatty acid and polyketide synthases.

5. Structural basis for substrate delivery by acyl carrier protein in the yeast fatty acid synthase.

6. Biosynthesis of lipid A precursors in Escherichia coli. A cytoplasmic acyltransferase that converts UDP-N-acetylglucosamine to UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine.

7. Crystal structure and acyl chain selectivity of Escherichia coli LpxD, the N-acyltransferase of lipid A biosynthesis.

8. Structure and reactivity of LpxD, the N-acyltransferase of lipid A biosynthesis.

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