This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2cla

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2cla.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2cla.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2cla| PDB=2cla | SCENE= }}
{{STRUCTURE_2cla| PDB=2cla | SCENE= }}
-
'''CRYSTAL STRUCTURE OF THE ASP-199-ASN MUTANT OF CHLORAMPHENICOL ACETYLTRANSFERASE TO 2.35 ANGSTROMS RESOLUTION. STRUCTURAL CONSEQUENCES OF DISRUPTION OF A BURIED SALT-BRIDGE'''
+
===CRYSTAL STRUCTURE OF THE ASP-199-ASN MUTANT OF CHLORAMPHENICOL ACETYLTRANSFERASE TO 2.35 ANGSTROMS RESOLUTION. STRUCTURAL CONSEQUENCES OF DISRUPTION OF A BURIED SALT-BRIDGE===
-
==Overview==
+
<!--
-
The crystal structure of the Asp-199----Asn mutant of chloramphenicol acetyltransferase (CAT) has been determined to 2.35-A resolution. In wild-type CAT Asp-199 is involved in a fully buried intrasubunit salt bridge with Arg-18, an interaction that is adjacent to the active site. Replacement of aspartate with asparagine by site-directed mutagenesis disrupts this salt bridge and causes extensive conformational changes within the active site. The imidazole group of the catalytically essential His-195 is reoriented, with the loss of interactions thought to stabilize the preferred tautomer of this residue. Arg-18 and Asn-199 form three new intersubunit interactions as a result of large side-chain torsion angle changes which cause the movement of two polypeptide loops, some residues of which are up to 20 A away from the site of the mutation. The new interactions of Arg-18 and Asn-199 compensate for the loss of the buried salt bridge and afford near-wild-type thermostability to Asn-199 CAT, albeit with a greatly reduced activity.
+
The line below this paragraph, {{ABSTRACT_PUBMED_2271709}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 2271709 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_2271709}}
==About this Structure==
==About this Structure==
Line 26: Line 30:
[[Category: Leslie, A G.W.]]
[[Category: Leslie, A G.W.]]
[[Category: Moody, P C.E.]]
[[Category: Moody, P C.E.]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 22:24:54 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 09:33:47 2008''

Revision as of 06:33, 29 July 2008

Image:2cla.png

Template:STRUCTURE 2cla

CRYSTAL STRUCTURE OF THE ASP-199-ASN MUTANT OF CHLORAMPHENICOL ACETYLTRANSFERASE TO 2.35 ANGSTROMS RESOLUTION. STRUCTURAL CONSEQUENCES OF DISRUPTION OF A BURIED SALT-BRIDGE

Template:ABSTRACT PUBMED 2271709

About this Structure

2CLA is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Crystal structure of the aspartic acid-199----asparagine mutant of chloramphenicol acetyltransferase to 2.35-A resolution: structural consequences of disruption of a buried salt bridge., Gibbs MR, Moody PC, Leslie AG, Biochemistry. 1990 Dec 25;29(51):11261-5. PMID:2271709

Page seeded by OCA on Tue Jul 29 09:33:47 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2cla"
Personal tools