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.


1f44

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1f44.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1f44.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1f44| PDB=1f44 | SCENE= }}
{{STRUCTURE_1f44| PDB=1f44 | SCENE= }}
-
'''CRYSTAL STRUCTURE OF TRIMERIC CRE RECOMBINASE-LOX COMPLEX'''
+
===CRYSTAL STRUCTURE OF TRIMERIC CRE RECOMBINASE-LOX COMPLEX===
-
==Overview==
+
<!--
-
The crystal structure of a novel Cre-Lox synapse was solved using phases from multiple isomorphous replacement and anomalous scattering, and refined to 2.05 A resolution. In this complex, a symmetric protein trimer is bound to a Y-shaped three-way DNA junction, a marked departure from the pseudo-4-fold symmetrical tetramer associated with Cre-mediated LoxP recombination. The three-way DNA junction was accommodated by a simple kink without significant distortion of the adjoining DNA duplexes. Although the mean angle between DNA arms in the Y and X structures was similar, adjacent Cre trimer subunits rotated 29 degrees relative to those in the tetramers. This rotation was accommodated at the protein-protein and DNA-DNA interfaces by interactions that are "quasi-equivalent" to those in the tetramer, analogous to packing differences of chemically identical viral subunits at non-equivalent positions in icosahedral capsids. This structural quasi-equivalence extends to function as Cre can bind to, cleave and perform strand transfer with a three-way Lox substrate. The structure explains the dual recognition of three and four-way junctions by site-specific recombinases as being due to shared structural features between the differently branched substrates and plasticity of the protein-protein interfaces. To our knowledge, this is the first direct demonstration of quasi-equivalence in both the assembly and function of an oligomeric enzyme.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11601846}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11601846 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11601846}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Trimeric]]
[[Category: Trimeric]]
[[Category: Y-junction]]
[[Category: Y-junction]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:52:24 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:39:11 2008''

Revision as of 23:39, 30 June 2008

Image:1f44.png

Template:STRUCTURE 1f44

CRYSTAL STRUCTURE OF TRIMERIC CRE RECOMBINASE-LOX COMPLEX

Template:ABSTRACT PUBMED 11601846

About this Structure

1F44 is a Single protein structure of sequence from Enterobacteria phage p1. Full crystallographic information is available from OCA.

Reference

Quasi-equivalence in site-specific recombinase structure and function: crystal structure and activity of trimeric Cre recombinase bound to a three-way Lox DNA junction., Woods KC, Martin SS, Chu VC, Baldwin EP, J Mol Biol. 2001 Oct 12;313(1):49-69. PMID:11601846

Page seeded by OCA on Tue Jul 1 02:39:11 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1f44"
Personal tools