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.


2ief

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2ief.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2ief.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2ief| PDB=2ief | SCENE= }}
{{STRUCTURE_2ief| PDB=2ief | SCENE= }}
-
'''Structure of the cooperative Excisionase (Xis)-DNA complex reveals a micronucleoprotein filament'''
+
===Structure of the cooperative Excisionase (Xis)-DNA complex reveals a micronucleoprotein filament===
-
==Overview==
+
<!--
-
The DNA architectural protein Xis regulates the construction of higher-order nucleoprotein intasomes that integrate and excise the genome of phage lambda from the Escherichia coli chromosome. Xis modulates the directionality of site-specific recombination by stimulating phage excision 10(6)-fold, while simultaneously inhibiting phage reintegration. Control is exerted by cooperatively assembling onto a approximately 35-bp DNA regulatory element, which it distorts to preferentially stabilize an excisive intasome. Here, we report the 2.6-A crystal structure of the complex between three cooperatively bound Xis proteins and a 33-bp DNA containing the regulatory element. Xis binds DNA in a head-to-tail orientation to generate a micronucleoprotein filament. Although each protomer is anchored to the duplex by a similar set of nonbase specific contacts, malleable protein-DNA interactions enable binding to sites that differ in nucleotide sequence. Proteins at the ends of the duplex sequence specifically recognize similar binding sites and participate in cooperative binding via protein-protein interactions with a bridging Xis protomer that is bound in a less specific manner. Formation of this polymer introduces approximately 72 degrees of curvature into the DNA with slight positive writhe, which functions to connect disparate segments of DNA bridged by integrase within the excisive intasome.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17287355}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17287355 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17287355}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Recombination directionality factor]]
[[Category: Recombination directionality factor]]
[[Category: Site specific recombination]]
[[Category: Site specific recombination]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:24:24 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:42:16 2008''

Revision as of 01:42, 28 July 2008

Image:2ief.png

Template:STRUCTURE 2ief

Structure of the cooperative Excisionase (Xis)-DNA complex reveals a micronucleoprotein filament

Template:ABSTRACT PUBMED 17287355

About this Structure

2IEF is a Single protein structure of sequence from Enterobacteria phage lambda. Full crystallographic information is available from OCA.

Reference

Structure of the cooperative Xis-DNA complex reveals a micronucleoprotein filament that regulates phage lambda intasome assembly., Abbani MA, Papagiannis CV, Sam MD, Cascio D, Johnson RC, Clubb RT, Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2109-14. Epub 2007 Feb 7. PMID:17287355

Page seeded by OCA on Mon Jul 28 04:42:16 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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