Charge neutralization in the active site of the catalytic trimer of aspartate transcarbamoylase promotes diverse structural changes-Reference-Cited by-同舟云学术

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Charge neutralization in the active site of the catalytic trimer of aspartate transcarbamoylase promotes diverse structural changes

Published:2017-09-30 Issue:11 Volume:26 Page:2221-2228
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Endrizzi James A.¹,Beernink Peter T.²³^ORCID

Affiliation:

1. Supernova C; Missoula Montana

2. Children's Hospital Oakland Research Institute; UCSF Benioff Children's Hospital; Oakland California

3. Department of Pediatrics, School of Medicine; University of California, San Francisco; San Francisco California

Funder

Office of Extramural Research, National Institutes of Health

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/pro.3277/fullpdf

Reference44 articles.

1. Glucose-induced conformational change in yeast hexokinase;Bennett;Proc Natl Acad Sci USA,1978

2. Binding of ligands to the active site of carboxypeptidase A;Rees;Proc Natl Acad Sci USA,1981

3. A mutant T4 lysozyme displays five different crystal conformations;Faber;Nature,1990

4. Crystal structures of substrates and products bound to the phosphoglycerate kinase active site reveal the catalytic mechanism;Bernstein;Biochemistry,1998

5. Conformational changes during the catalytic cycle of gluconate kinase as revealed by X-ray crystallography;Kraft;J Mol Biol,2002

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