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.

2caj

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2caj.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2caj.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2caj| PDB=2caj | SCENE= }}
{{STRUCTURE_2caj| PDB=2caj | SCENE= }}
-
'''NIKR FROM HELICOBACTER PYLORI IN CLOSED TRANS-CONFORMATION AND NICKEL BOUND TO 4 INTERMEDIARY SITES'''
+
===NIKR FROM HELICOBACTER PYLORI IN CLOSED TRANS-CONFORMATION AND NICKEL BOUND TO 4 INTERMEDIARY SITES===
-
==Overview==
+
<!--
-
The survival of Helicobacter pylori in the human stomach critically relies on the availability and use of nickel, an absolute cofactor of the important virulence determinant urease. Nickel-responsive gene regulation is mediated by HpNikR, a protein belonging to the ribbon-helix-helix family of transcriptional regulators. Unlike its homologues, HpNikR acts as both a repressor and an activator within an acid adaptation cascade. We report the crystal structure of the full-length HpNikR in a nickel-free conformation and two nickel-bound structures obtained in different conditions: Ni1-HpNikR and Ni2-HpNikR. Apo-HpNikR shows the same global fold as its bacterial homologues although with an unusual closed trans-conformation and asymmetrical quaternary arrangement. The structure of Ni1-HpNikR in the presence of nickel has two different sides, one showing nickel binding similar to that of known NikRs and the other reflecting an intermediate state. The structure of Ni2-HpNikR obtained using a shorter exposure to nickel provides another snapshot of the nickel incorporation. Altogether, the three structures have allowed us to determine the route for nickel within HpNikR and reveal the cooperativity between the tetramerization domain and the DNA-binding domain. Experiments using point mutations of HpnikR residues involved in nickel internalisation confirm that these residues are critical for HpNikR functions in vivo.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16872629}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16872629 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16872629}}
==About this Structure==
==About this Structure==
Line 37: Line 41:
[[Category: Transcription regulator]]
[[Category: Transcription regulator]]
[[Category: Transcriptional regulation]]
[[Category: Transcriptional regulation]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 21:34:49 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 21:12:59 2008''

Revision as of 18:13, 28 July 2008

Template:STRUCTURE 2caj

NIKR FROM HELICOBACTER PYLORI IN CLOSED TRANS-CONFORMATION AND NICKEL BOUND TO 4 INTERMEDIARY SITES

Template:ABSTRACT PUBMED 16872629

About this Structure

2CAJ is a Single protein structure of sequence from Helicobacter pylori. Full crystallographic information is available from OCA.

Reference

Structural basis of the nickel response in Helicobacter pylori: crystal structures of HpNikR in Apo and nickel-bound states., Dian C, Schauer K, Kapp U, McSweeney SM, Labigne A, Terradot L, J Mol Biol. 2006 Aug 25;361(4):715-30. Epub 2006 Jul 7. PMID:16872629

Page seeded by OCA on Mon Jul 28 21:12:59 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools