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.


1k56

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1k56.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1k56.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1k56| PDB=1k56 | SCENE= }}
{{STRUCTURE_1k56| PDB=1k56 | SCENE= }}
-
'''OXA 10 class D beta-lactamase at pH 6.5'''
+
===OXA 10 class D beta-lactamase at pH 6.5===
-
==Overview==
+
<!--
-
beta-Lactamases are the resistance enzymes for beta-lactam antibiotics, of which four classes are known. beta-lactamases hydrolyze the beta-lactam moieties of these antibiotics, rendering them inactive. It is shown herein that the class D OXA-10 beta-lactamase depends critically on an unusual carbamylated lysine as the basic residue for both the enzyme acylation and deacylation steps of catalysis. The formation of carbamylated lysine is reversible. Evidence is presented that this enzyme is dimeric and carbamylated in living bacteria. High-resolution x-ray structures for the native enzyme were determined at pH values of 6.0, 6.5, 7.5, and 8.5. Two dimers are present per asymmetric unit. One monomer in each dimer was carbamylated at pH 6.0, whereas all four monomers were fully carbamylated at pH 8.5. At the intermediate pH values, one monomer of each dimer was carbamylated, and the other showed a mixture of carbamylated and non-carbamylated lysines. It would appear that, as the pH increased for the sample, additional lysines were "titrated" by carbamylation. A handful of carbamylated lysines are known from protein crystallographic data, all of which have been attributed roles in structural stabilization (mostly as metal ligands) of the proteins. This paper reports a previously unrecognized role for a noncoordinated carbamylate lysine as a basic residue involved in mechanistic reactions of an enzyme, which indicates another means for expansion of the catalytic capabilities of the amino acids in nature beyond the 20 common amino acids in development of biological catalysts.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11724923}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11724923 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11724923}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Beta-lactamase]]
[[Category: Beta-lactamase]]
[[Category: Carbamylation]]
[[Category: Carbamylation]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:19:23 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 09:47:57 2008''

Revision as of 06:47, 2 July 2008

Image:1k56.png

Template:STRUCTURE 1k56

OXA 10 class D beta-lactamase at pH 6.5

Template:ABSTRACT PUBMED 11724923

About this Structure

1K56 is a Protein complex structure of sequences from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.

Reference

Critical involvement of a carbamylated lysine in catalytic function of class D beta-lactamases., Golemi D, Maveyraud L, Vakulenko S, Samama JP, Mobashery S, Proc Natl Acad Sci U S A. 2001 Dec 4;98(25):14280-5. Epub 2001 Nov 27. PMID:11724923

Page seeded by OCA on Wed Jul 2 09:47:57 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1k56"
Personal tools