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.


1m6x

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1m6x.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1m6x.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1m6x| PDB=1m6x | SCENE= }}
{{STRUCTURE_1m6x| PDB=1m6x | SCENE= }}
-
'''Flpe-Holliday Junction Complex'''
+
===Flpe-Holliday Junction Complex===
-
==Overview==
+
<!--
-
The Flp recombinase, a member of the lambda integrase or tyrosine-based family of site-specific recombinases, is an interesting example of an enzyme whose catalytic activity is regulated by protein-protein contacts. It exhibits half-of-the-sites activity throughout its catalytic cycle. Flp is unique among these recombinases, in that it assembles each active site in trans through the interaction of two protein monomers within the catalytic tetramer, with isomerization of interacting pairs being essential to complete a full reaction. We report here the structure of a DNA-bound tetramer of Flpe, a variant of Flp that is more active at 37 degrees C than the wild-type recombinase. This new structure includes the first observation of a tyrosine recombinase with an invading 5'-OH poised to attack the covalent phosphotyrosine residue. Comparison with the previously determined Flp structure highlights differences in flexibility between the two types of protein-protein interfaces in the tetramer and better defines the range of conformations available to this remarkably flexible complex. These results suggest a steric occlusion model for enforcement of half-of-the-sites activity.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12559911}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12559911 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12559911}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Protein-dna complex]]
[[Category: Protein-dna complex]]
[[Category: Tyrosine recombinase]]
[[Category: Tyrosine recombinase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:42:43 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 23:20:52 2008''

Revision as of 20:20, 2 July 2008

Image:1m6x.png

Template:STRUCTURE 1m6x

Flpe-Holliday Junction Complex

Template:ABSTRACT PUBMED 12559911

About this Structure

1M6X is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Structural plasticity of the Flp-Holliday junction complex., Conway AB, Chen Y, Rice PA, J Mol Biol. 2003 Feb 14;326(2):425-34. PMID:12559911

Page seeded by OCA on Wed Jul 2 23:20:52 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1m6x"
Personal tools