ATPase Active-Site Electrostatic Interactions Control the Global Conformation of the 100 kDa SecA Translocase-Reference-Cited by-同舟云学术

ATPase Active-Site Electrostatic Interactions Control the Global Conformation of the 100 kDa SecA Translocase

Published:2013-02-14 Issue:8 Volume:135 Page:2999-3010
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Kim Dorothy M.¹²,Zheng Haiyan³⁴,Huang Yuanpeng J.³,Montelione Gaetano T.³⁴,Hunt John F.¹

Affiliation:

1. Department of Biological Sciences and Northeast Structural Genomics Consortium, 702A Fairchild Center, MC2434, Columbia University, New York, New York 10027, United States

2. Department of Biochemistry and Molecular Biophysics, Columbia University, 650 West 168th Street, New York, New York 10032, United States

3. Center for Advanced Biotechnology and Medicine, Department of Molecular Biology and Biochemistry, and Northeast Structural Genomics Consortium, Rutgers, The State University of New Jersey, Piscataway, New Jersey 08854, United States

4. Department of Biochemistry and Molecular Biology, Robert Wood Johnson Medical School, University of Medicine and Dentistry of New Jersey, Piscataway, New Jersey 08854, United States

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja306361q

Reference68 articles.

1. Homology in amino-terminal sequence of precursors to pancreatic secretory proteins.

2. Identification of a new gene (secA) and gene product involved in the secretion of envelope proteins in Escherichia coli

3. Suppressor analysis suggests a multistep, cyclic mechanism for protein secretion in Escherichia coli.

4. Suppression of signal sequence defects and azide resistance in Escherichia coli commonly result from the same mutations in secA

5. The purified E. coli integral membrane protein SecYE is sufficient for reconstitution of SecA-dependent precursor protein translocation

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