CaltechAUTHORS
  A Caltech Library Service

Refined Crystal Structure of the Potato Inhibitor Complex of Carboxypeptidase A at 2.5 Å Resolution

Rees, D. C. and Lipscomb, W. N. (1982) Refined Crystal Structure of the Potato Inhibitor Complex of Carboxypeptidase A at 2.5 Å Resolution. Journal of Molecular Biology, 160 (3). pp. 475-498. ISSN 0022-2836. http://resolver.caltech.edu/CaltechAUTHORS:20150210-100044543

Full text is not posted in this repository. Consult Related URLs below.

Use this Persistent URL to link to this item: http://resolver.caltech.edu/CaltechAUTHORS:20150210-100044543

Abstract

The exopeptidase carboxypeptidase A forms a tight complex with a 39 residue inhibitor protein from potatoes. We have determined the crystal structure of this complex, and refined the atomic model to a crystallographic R-factor of 0.196 at 2.5 Å resolution. The structure of the inhibitor protein is organized around a core of disulfide bridges. No α-helices or β-sheets are present in this protein, although there is one turn of 3_(10) helix. The four carboxy-terminal residues of the inhibitor protein bind in the active site groove of carboxypeptidase A, defining binding subsites S′_1, S_1, S_2 and S_3 on the enzyme. The carboxy-terminal glycine of the inhibitor is cleaved from the remainder of the inhibitor in the complex, and remains trapped in the back of the active site pocket. Interactions between the inhibitor and residues Tyr248 and Arg71 of carboxypeptidase A resemble possible features of binding stages for substrates both prior and subsequent to peptide bond hydrolysis. Not all of these interactions would be available to different types of ester substrates, however, which may be in part responsible for the observed kinetic differences in hydrolysis between peptides and various classes of esters. With the exception of residues involved in the binding of the inhibitor protein (such as Tyr248), the structure of carboxypeptidase A as determined in the inhibitor complex is quite similar to the structure of the unliganded enzyme (Lipscomb et al., 1968), which was solved from an unrelated crystal form.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1016/0022-2836(82)90309-6DOIArticle
http://www.sciencedirect.com/science/article/pii/0022283682903096PublisherArticle
ORCID:
AuthorORCID
Rees, D. C.0000-0002-1076-1503
Additional Information:© 1982 Academic Press Inc. (London) Ltd. Received 6 October 1981, and in revised form. 13 May 1982. We acknowledge the contribution of Dr. M. Lewis to the refinement work, and Drs. J.E. Ladner, R.C. Ladner and G. Shoham for the graphics programs. This work has been supported by National Institutes of Health grant GM-06920; National Science Foundation grant PCM-77-11398 supported the computational facilities.
Funders:
Funding AgencyGrant Number
NIHGM-06920
NSFPCM-77-11398
Record Number:CaltechAUTHORS:20150210-100044543
Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:20150210-100044543
Official Citation:D.C. Rees, W.N. Lipscomb, Refined crystal structure of the potato inhibitor complex of carboxypeptidase A at 2.5 Å resolution, Journal of Molecular Biology, Volume 160, Issue 3, 25 September 1982, Pages 475-498, ISSN 0022-2836, http://dx.doi.org/10.1016/0022-2836(82)90309-6. (http://www.sciencedirect.com/science/article/pii/0022283682903096)
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:54651
Collection:CaltechAUTHORS
Deposited By: SWORD User
Deposited On:11 Feb 2015 00:06
Last Modified:21 Nov 2017 19:05

Repository Staff Only: item control page