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PMID: 6930653 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Structure of a mycobacterial polysaccharide-fatty acyl-CoA complex: nuclear magnetic resonance studies.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 77 ·No. 5 ·1980-05-00 ·Pages 2582-6

Maggio JE

Abstract

MMP, a linear alpha 1 leads to 4 linked polymer of 3-O-methylmannose, regulates the fatty acid synthetase from Mycobacterium smegmatis by forming stoichiometric complexes with the long-chain acyl-CoA synthetase products. In agreement with previous proposals [Bloch, K. (1977) in Advances in Enzymology and Related Areas of Molecular Biology, ed. Meister, A. (Wiley, New York), Vol. 45, pp. 1-84], nuclear magnetic resonance studies show that the polysaccharide, a random coil in its free form, undergoes a major conformational transition upon enclosing long-chain acyl-CoA. The polysaccharide, probably in helical conformation in the complexed form, interacts with both the paraffinic chain and the CoA moieties of the included fatty acyl thioester.

MeSH Terms

Acyl Coenzyme A Binding Sites Magnetic Resonance Spectroscopy Mannosides Molecular Conformation Mycobacterium Palmitates Polysaccharides, Bacterial Structure-Activity Relationship

Chemicals

Acyl Coenzyme A Mannosides Palmitates Polysaccharides, Bacterial

Authors & Affiliations

1 authors, click to expand affiliations / ORCID

Maggio J E

References (22)

22 references, click to expand

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Article Info

Journal

Proceedings of the National Academy of Sciences of the United States of America

Abbr.

Proc Natl Acad Sci U S A

ISSN

0027-8424

DOI

10.1073/pnas.77.5.2582

Published

1980-05-00

Pages

2582-6

Language

English

Region

United States

NLM ID

7505876

PMCID

PMC349446

Subset

External Links

PubMed source DOI: 10.1073/pnas.77.5.2582 PMC Full Text View journal details

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Structure of a mycobacterial polysaccharide-fatty acyl-CoA complex: nuclear magnetic resonance studies.

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