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.


2hq5

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2hq5.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2hq5.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2hq5| PDB=2hq5 | SCENE= }}
{{STRUCTURE_2hq5| PDB=2hq5 | SCENE= }}
-
'''Crystal structure of multidrug binding protein QacR from Staphylococcus aureus cocrystallized with compound DB359'''
+
===Crystal structure of multidrug binding protein QacR from Staphylococcus aureus cocrystallized with compound DB359===
-
==Overview==
+
<!--
-
Staphylococcus aureus QacR is a multidrug-binding transcription repressor. Crystal structures of multiple QacR-drug complexes reveal that these toxins bind in a large pocket, which is composed of smaller overlapping "minipockets". Stacking, van der Waals, and ionic interactions are common features of binding, whereas hydrogen bonds are limited. Pentamidine, a bivalent aromatic diamidine, interacts with QacR differently as one positively charged benzamidine moiety is neutralized by the dipoles of side-chain and peptide backbone oxygens rather than a formal negative charge from proximal acidic residues. To understand the binding mechanisms of other bivalent benzamidines, we determined the crystal structures of the QacR-DB75 and QacR-DB359 complexes and measured their binding affinities. Although these rigid aromatic diamidines bind with low-micromolar affinities, they do not use single, discrete binding modes. Such promiscuous binding underscores the intrinsic chemical redundancy of the QacR multidrug-binding pocket. Chemical redundancy is likely a hallmark of all multidrug-binding pockets, yet it is utilized by only a subset of drugs, which, for QacR, so far appears to be limited to chemically rigid, bivalent compounds.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17567017}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17567017 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17567017}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Multidrug recognition]]
[[Category: Multidrug recognition]]
[[Category: Qacr]]
[[Category: Qacr]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:34:15 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:43:25 2008''

Revision as of 14:43, 27 July 2008

Image:2hq5.png

Template:STRUCTURE 2hq5

Crystal structure of multidrug binding protein QacR from Staphylococcus aureus cocrystallized with compound DB359

Template:ABSTRACT PUBMED 17567017

About this Structure

2HQ5 is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.

Reference

Multidrug-binding transcription factor QacR binds the bivalent aromatic diamidines DB75 and DB359 in multiple positions., Brooks BE, Piro KM, Brennan RG, J Am Chem Soc. 2007 Jul 4;129(26):8389-95. Epub 2007 Jun 13. PMID:17567017

Page seeded by OCA on Sun Jul 27 17:43:25 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2hq5"
Personal tools