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.


2pmu

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2pmu.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2pmu.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2pmu| PDB=2pmu | SCENE= }}
{{STRUCTURE_2pmu| PDB=2pmu | SCENE= }}
-
'''Crystal structure of the DNA-binding domain of PhoP'''
+
===Crystal structure of the DNA-binding domain of PhoP===
-
==Overview==
+
<!--
-
The PhoP-PhoR two-component signaling system from Mycobacterium tuberculosis is essential for the virulence of the tubercle bacillus. The response regulator, PhoP, regulates expression of over 110 genes. In order to elucidate the regulatory mechanism of PhoP, we determined the crystal structure of its DNA-binding domain (PhoPC). PhoPC exhibits a typical fold of the winged helix-turn-helix subfamily of response regulators. The structure starts with a four-stranded antiparallel beta-sheet, followed by a three-helical bundle of alpha-helices, and then a C-terminal beta-hairpin, which together with a short beta-strand between the first and second helices forms a three-stranded antiparallel beta-sheet. Structural elements are packed through a hydrophobic core, with the first helix providing a scaffold for the rest of the domain to pack. The second and third helices and the long, flexible loop between them form the helix-turn-helix motif, with the third helix being the recognition helix. The C-terminal beta-hairpin turn forms the wing motif. The molecular surfaces around the recognition helix and the wing residues show strong positive electrostatic potential, consistent with their roles in DNA binding and nucleotide sequence recognition. The crystal packing of PhoPC gives a hexamer ring, with neighboring molecules interacting in a head-to-tail fashion. This packing interface suggests that PhoPC could bind DNA in a tandem association. However, this mode of DNA binding is likely to be nonspecific because the recognition helix is partially blocked and would be prevented from inserting into the major groove of DNA. Detailed structural analysis and implications with respect to DNA binding are discussed.
+
The line below this paragraph, {{ABSTRACT_PUBMED_18052041}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 18052041 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_18052041}}
==About this Structure==
==About this Structure==
Line 25: Line 29:
[[Category: Transcription regulation]]
[[Category: Transcription regulation]]
[[Category: Winged helix-tun-helx]]
[[Category: Winged helix-tun-helx]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 13:26:31 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 12:59:03 2008''

Revision as of 09:59, 28 July 2008

Image:2pmu.png

Template:STRUCTURE 2pmu

Crystal structure of the DNA-binding domain of PhoP

Template:ABSTRACT PUBMED 18052041

About this Structure

2PMU is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

Reference

Structure of the DNA-binding domain of the response regulator PhoP from Mycobacterium tuberculosis., Wang S, Engohang-Ndong J, Smith I, Biochemistry. 2007 Dec 25;46(51):14751-61. Epub 2007 Dec 1. PMID:18052041

Page seeded by OCA on Mon Jul 28 12:59:03 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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