1f36

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1f36.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1f36.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1f36| PDB=1f36 | SCENE= }}
{{STRUCTURE_1f36| PDB=1f36 | SCENE= }}
-
'''THE CRYSTAL STRUCTURE OF FIS MUTANT K36E REVEALS THAT THE TRANSACTIVATION REGION OF THE FIS PROTEIN CONTAINS EXTENDED MOBILE BETA-HAIRPIN ARMS'''
+
===THE CRYSTAL STRUCTURE OF FIS MUTANT K36E REVEALS THAT THE TRANSACTIVATION REGION OF THE FIS PROTEIN CONTAINS EXTENDED MOBILE BETA-HAIRPIN ARMS===
-
==Overview==
+
<!--
-
The Fis protein regulates site-specific DNA inversion catalyzed by a family of DNA invertases when bound to a cis-acting recombinational enhancer. As is often found for transactivation domains, previous crystal structures have failed to resolve the conformation of the N-terminal inversion activation region within the Fis dimer. A new crystal form of a mutant Fis protein now reveals that the activation region contains two beta-hairpin arms that protrude over 20 A from the protein core. Saturation mutagenesis identified the regulatory and structurally important amino acids. The most critical activating residues are located near the tips of the beta-arms. Disulfide cross-linking between the beta-arms demonstrated that they are highly flexible in solution and that efficient inversion activation can occur when the beta-arms are covalently linked together. The emerging picture for this regulatory motif is that contacts with the recombinase at the tip of the mobile beta-arms activate the DNA invertase in the context of an invertasome complex.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9362499}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9362499 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9362499}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Protein-protein interaction domain]]
[[Category: Protein-protein interaction domain]]
[[Category: Transactivation region]]
[[Category: Transactivation region]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:50:13 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:35:23 2008''

Revision as of 23:35, 30 June 2008

Template:STRUCTURE 1f36

THE CRYSTAL STRUCTURE OF FIS MUTANT K36E REVEALS THAT THE TRANSACTIVATION REGION OF THE FIS PROTEIN CONTAINS EXTENDED MOBILE BETA-HAIRPIN ARMS

Template:ABSTRACT PUBMED 9362499

About this Structure

1F36 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

The transactivation region of the fis protein that controls site-specific DNA inversion contains extended mobile beta-hairpin arms., Safo MK, Yang WZ, Corselli L, Cramton SE, Yuan HS, Johnson RC, EMBO J. 1997 Nov 17;16(22):6860-73. PMID:9362499

Page seeded by OCA on Tue Jul 1 02:35:23 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools