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PMID: 11756679 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Quaternary structure of human fatty acid synthase by electron cryomicroscopy.

Brink J, Ludtke SJ, Yang CY, Gu ZW, Wakil SJ, Chiu W

Abstract

We present the first three-dimensional reconstruction of human fatty acid synthase obtained by electron cryomicroscopy and single-particle image processing. The structure shows that the synthase is composed of two monomers, arranged in an antiparallel orientation, which is consistent with biochemical data. The monomers are connected to each other at their middle by a bridge of density, a site proposed to be the combination of the interdomain regions of the two monomers. Each monomer subunit appears to be subdivided into three structural domains. With this reconstruction of the synthase, we propose a location for the enzyme's two fatty acid synthesis sites.

MeSH Terms
Binding Sites Cryoelectron Microscopy Electrophoresis, Polyacrylamide Gel Fatty Acid Synthases/chemistry Humans Protein Structure, Quaternary Protein Structure, Tertiary Scattering, Radiation Tumor Cells, Cultured X-Rays
Chemicals
Fatty Acid Synthases
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Brink Jacob
Verna and Marrs McLean Department of Biochemistry and Molecular Biology and National Center for Macromolecular Imaging, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA.
Ludtke Steven J
Yang Chao-Yuh
Gu Zei-Wei
Wakil Salih J
Chiu Wah
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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
Published
2002-01-08
Epub
2001-00-26
Pages
138-43
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC117528
Subset
IM
Grants
NCRR NIH HHS · P41 RR002250 · United States
NIGMS NIH HHS · GMS19091 · United States
NCRR NIH HHS · P41RR012109 · United States
NCRR NIH HHS · P41RR02250 · United States
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