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.


1r1v

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1r1v.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1r1v.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1r1v| PDB=1r1v | SCENE= }}
{{STRUCTURE_1r1v| PDB=1r1v | SCENE= }}
-
'''Crystal structure of the metal-sensing transcriptional repressor CzrA from Staphylococcus aureus in the Zn2-form'''
+
===Crystal structure of the metal-sensing transcriptional repressor CzrA from Staphylococcus aureus in the Zn2-form===
-
==Overview==
+
<!--
-
The origin of metal ion selectivity by members of the SmtB/ArsR family of bacterial metal-sensing transcriptional repressors and the mechanism of negative allosteric regulation of DNA binding is poorly understood. Here, we report that two homologous zinc sensors, Staphylococcus aureus CzrA and cyanobacterial SmtB, are "winged" helix homodimeric DNA-binding proteins that bind Zn(II) to a pair of tetrahedral, interhelical binding sites, with two ligands derived from the alpha5 helix of one subunit, Asp84 O(delta1) (Asp104 in SmtB), His86 N(delta1) (His106), and two derived from the alpha5 helix of the other, His97' N(delta1) (His117') and His100' N(epsilon2) (Glu120'). Formation of the metal chelate drives a quaternary structural switch mediated by an intersubunit hydrogen-binding network that originates with the non-liganding N(epsilon2) face of His97 in CzrA (His117 in SmtB) that stabilizes a low-affinity, DNA-binding conformation. The structure of the Zn(1) SmtB homodimer shows that both metal-binding sites of the dimer must be occupied for the quaternary structural switch to occur. Thus, a critical zinc-ligating histidine residue obligatorily couples formation of the metal-sensing coordination chelate to changes in the conformation and dynamics of the putative DNA-binding helices.
+
The line below this paragraph, {{ABSTRACT_PUBMED_14568530}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 14568530 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_14568530}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Winged hth protein]]
[[Category: Winged hth protein]]
[[Category: Zinc]]
[[Category: Zinc]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:58:21 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:57:17 2008''

Revision as of 18:57, 27 July 2008

Image:1r1v.png

Template:STRUCTURE 1r1v

Crystal structure of the metal-sensing transcriptional repressor CzrA from Staphylococcus aureus in the Zn2-form

Template:ABSTRACT PUBMED 14568530

About this Structure

1R1V is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.

Reference

A metal-ligand-mediated intersubunit allosteric switch in related SmtB/ArsR zinc sensor proteins., Eicken C, Pennella MA, Chen X, Koshlap KM, VanZile ML, Sacchettini JC, Giedroc DP, J Mol Biol. 2003 Oct 31;333(4):683-95. PMID:14568530

Page seeded by OCA on Sun Jul 27 21:57:17 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1r1v"
Personal tools