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.


1xa1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1xa1.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1xa1.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1xa1| PDB=1xa1 | SCENE= }}
{{STRUCTURE_1xa1| PDB=1xa1 | SCENE= }}
-
'''Crystal structure of the sensor domain of BlaR1 from Staphylococcus aureus in its apo form'''
+
===Crystal structure of the sensor domain of BlaR1 from Staphylococcus aureus in its apo form===
-
==Overview==
+
<!--
-
Staphylococcus aureus is among the most prevalent and antibiotic-resistant of pathogenic bacteria. The resistance of S. aureus to prototypal beta-lactam antibiotics is conferred by two mechanisms: (i) secretion of hydrolytic beta-lactamase enzymes and (ii) production of beta-lactam-insensitive penicillin-binding proteins (PBP2a). Despite their distinct modes of resistance, expression of these proteins is controlled by similar regulation systems, including a repressor (BlaI/MecI) and a multidomain transmembrane receptor (BlaR1/MecR1). Resistance is triggered in response to a covalent binding event between a beta-lactam antibiotic and the extracellular sensor domain of BlaR1/MecR1 by transduction of the binding signal to an intracellular protease domain capable of repressor inactivation. This study describes the first crystal structures of the sensor domain of BlaR1 (BlaRS) from S. aureus in both the apo and penicillin-acylated forms. The structures show that the sensor domain resembles the beta-lactam-hydrolyzing class D beta-lactamases, but is rendered a penicillin-binding protein due to the formation of a very stable acyl-enzyme. Surprisingly, conformational changes upon penicillin binding were not observed in our structures, supporting the hypothesis that transduction of the antibiotic-binding signal into the cytosol is mediated by additional intramolecular interactions of the sensor domain with an adjacent extracellular loop in BlaR1.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15322076}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15322076 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15322076}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Sensor domain]]
[[Category: Sensor domain]]
[[Category: Staphylococcus aureus]]
[[Category: Staphylococcus aureus]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 14:45:56 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:05:55 2008''

Revision as of 16:06, 27 July 2008

Image:1xa1.png

Template:STRUCTURE 1xa1

Crystal structure of the sensor domain of BlaR1 from Staphylococcus aureus in its apo form

Template:ABSTRACT PUBMED 15322076

About this Structure

1XA1 is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.

Reference

Crystal structures of the Apo and penicillin-acylated forms of the BlaR1 beta-lactam sensor of Staphylococcus aureus., Wilke MS, Hills TL, Zhang HZ, Chambers HF, Strynadka NC, J Biol Chem. 2004 Nov 5;279(45):47278-87. Epub 2004 Aug 18. PMID:15322076

Page seeded by OCA on Sun Jul 27 19:05:55 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1xa1"
Personal tools