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Crystallographic Studies on Apocarboxypeptidase A and the Complex with Glycyl-L-Tyrosine

Rees, D. C. and Lipscomb, W. N. (1983) Crystallographic Studies on Apocarboxypeptidase A and the Complex with Glycyl-L-Tyrosine. Proceedings of the National Academy of Sciences of the United States of America, 80 (23). pp. 7151-7154. ISSN 0027-8424. PMCID PMC390011. https://resolver.caltech.edu/CaltechAUTHORS:20150210-095316855

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Abstract

The crystal structures of zinc-free carboxypeptidase A (apocarboxypeptidase A) and the complex of glycyl-L-tyrosine with apocarboxypeptidase A are described and compared to the corresponding structures of the zinc-containing enzyme. Only small conformational changes in the zinc ligands accompany removal of the metal. Interactions between the tyrosine residue of glycyl-L-tyrosine and apocarboxypeptidase A are similar to those observed in the complex with the holoenzyme. However, in the absence of zinc, the carbonyl oxygen of the glycyl moiety now receives a hydrogen bond from the side chain of arginine-127. Although not as yet observed, a similar shift of the carbonyl oxygen of a susceptible bond from the zinc to arginine-127 could stabilize tetrahedral intermediates generated during the hydrolysis of substrates by carboxypeptidase.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://www.pnas.org/content/80/23/7151PublisherArticle
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC390011/PubMed CentralArticle
ORCID:
AuthorORCID
Rees, D. C.0000-0003-4073-1185
Contact Email Address:phoebe@caltech.edu
Additional Information:© 1983 National Academy of Sciences. Communicated by Konrad Bloch, August 22, 1983. We thank the National Institutes of Health (Grant GM 06920) and the Dreyfus Foundation (D.C.R.) for support. The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.
Funders:
Funding AgencyGrant Number
NIHGM 06920
Camille and Henry Dreyfus FoundationUNSPECIFIED
Subject Keywords:enzyme activity; proteases; protein crystallography; metalloproteins
Issue or Number:23
PubMed Central ID:PMC390011
Record Number:CaltechAUTHORS:20150210-095316855
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20150210-095316855
Official Citation:D C Rees and W N Lipscomb Crystallographic studies on apocarboxypeptidase A and the complex with glycyl-L-tyrosine PNAS 1983 80 (23) 7151-7154
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:54645
Collection:CaltechAUTHORS
Deposited By: SWORD User
Deposited On:11 Feb 2015 00:13
Last Modified:03 Oct 2019 07:59

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