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.


1hjp

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1hjp.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1hjp.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1hjp| PDB=1hjp | SCENE= }}
{{STRUCTURE_1hjp| PDB=1hjp | SCENE= }}
-
'''HOLLIDAY JUNCTION BINDING PROTEIN RUVA FROM E. COLI'''
+
===HOLLIDAY JUNCTION BINDING PROTEIN RUVA FROM E. COLI===
-
==Overview==
+
<!--
-
BACKGROUND: Homologous recombination is crucial for genetic diversity and repairing damaged chromosomes. In Escherichia coli cells, the RuvA, RuvB and RuvC proteins participate in the processing of an important intermediate, the Holliday junction. The RuvA-RuvB protein complex facilitates branch migration of the junction, depending on ATP hydrolysis. The atomic structure of RuvA should enable critical questions to be addressed about its specific interactions with the Holliday junction and the RuvB protein. RESULTS: The crystal structure of RuvA shows the tetrameric molecules with a fourfold axis at the center. Each subunit consists of three distinct domains, some of which contain important secondary structure elements for DNA binding. Together with the detailed structural information, the biochemical assays of various mutant RuvA proteins and domains, isolated by partial proteolysis, allowed us to define the functional roles of these domains in Holliday junction binding and the RuvB interaction. CONCLUSIONS: The RuvA molecule is formed by four identical subunits, each with three domains, I, II and III. The locations of the putative DNA-binding motifs define an interface between the DNA and the Holliday junction. Domain III is weakly attached to the core region, comprising domains I and II; the core domains can form a tetramer in the absence of domain III. Functional analyses of the mutant proteins and the partial digestion products, including Holliday junction binding and branch-migration assays, revealed that domain III and the preceding loop are crucial for RuvB binding and branch migration, although this region is not required for the junction-DNA binding.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9493263}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9493263 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9493263}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Dna repair]]
[[Category: Dna repair]]
[[Category: Holliday junction binding]]
[[Category: Holliday junction binding]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:55:02 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:16:45 2008''

Revision as of 05:16, 1 July 2008

Image:1hjp.png

Template:STRUCTURE 1hjp

HOLLIDAY JUNCTION BINDING PROTEIN RUVA FROM E. COLI

Template:ABSTRACT PUBMED 9493263

About this Structure

1HJP is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Functional analyses of the domain structure in the Holliday junction binding protein RuvA., Nishino T, Ariyoshi M, Iwasaki H, Shinagawa H, Morikawa K, Structure. 1998 Jan 15;6(1):11-21. PMID:9493263

Page seeded by OCA on Tue Jul 1 08:16:45 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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