We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1g6a

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1g6a.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1g6a.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1g6a| PDB=1g6a | SCENE= }}
{{STRUCTURE_1g6a| PDB=1g6a | SCENE= }}
-
'''PSE-4 CARBENICILLINASE, R234K MUTANT'''
+
===PSE-4 CARBENICILLINASE, R234K MUTANT===
-
==Overview==
+
<!--
-
PSE-4 is a class A beta-lactamase produced by strains of Pseudomonas aeruginosa and is highly active for the penicillin derivative carbenicillin. The crystal structure of the wild-type PSE-4 carbenicillinase has been determined to 1.95 A resolution by molecular replacement and represents the first structure of a carbenicillinase published to date. A superposition of the PSE-4 structure with that of TEM-1 shows a rms deviation of 1.3 A for 263 Calpha atoms. Most carbenicillinases are unique among class A beta-lactamases in that residue 234 is an arginine (ABL standard numbering scheme), while in all other class A enzymes this residue is a lysine. Kinetic characterization of a R234K PSE-4 mutant reveals a 50-fold reduction in k(cat)/K(m) and confirms the importance of Arg 234 for carbenicillinase activity. A comparison of the structure of the R234K mutant refined to 1.75 A resolution with the wild-type structure shows that Arg 234 stabilizes an alternate conformation of the Ser 130 side chain, not seen in other class A beta-lactamase structures. Our molecular modeling studies suggest that the position of a bound carbenicillin would be shifted relative to that of a bound benzylpenicillin in order to avoid a steric clash between the carbenicillin alpha-carboxylate group and the conserved side chain of Asn 170. The alternate conformation of the catalytic Ser 130 in wild-type PSE-4 may be involved in accommodating this shift in the bound substrate position.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11148033}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11148033 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11148033}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Class a beta-lactamase]]
[[Category: Class a beta-lactamase]]
[[Category: R234k mutant]]
[[Category: R234k mutant]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:11:38 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 04:41:29 2008''

Revision as of 01:41, 1 July 2008

Image:1g6a.png

Template:STRUCTURE 1g6a

PSE-4 CARBENICILLINASE, R234K MUTANT

Template:ABSTRACT PUBMED 11148033

About this Structure

1G6A is a Single protein structure of sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.

Reference

Insights into the molecular basis for the carbenicillinase activity of PSE-4 beta-lactamase from crystallographic and kinetic studies., Lim D, Sanschagrin F, Passmore L, De Castro L, Levesque RC, Strynadka NC, Biochemistry. 2001 Jan 16;40(2):395-402. PMID:11148033

Page seeded by OCA on Tue Jul 1 04:41:29 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1g6a"
Personal tools