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.


2ht1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2ht1.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2ht1.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2ht1| PDB=2ht1 | SCENE= }}
{{STRUCTURE_2ht1| PDB=2ht1 | SCENE= }}
-
'''The closed ring structure of the Rho transcription termination factor in complex with nucleic acid in the motor domains'''
+
===The closed ring structure of the Rho transcription termination factor in complex with nucleic acid in the motor domains===
-
==Overview==
+
<!--
-
Hexameric helicases and translocases are required for numerous essential nucleic-acid transactions. To better understand the mechanisms by which these enzymes recognize target substrates and use nucleotide hydrolysis to power molecular movement, we have determined the structure of the Rho transcription termination factor, a hexameric RNA/DNA helicase, with single-stranded RNA bound to the motor domains of the protein. The structure reveals a closed-ring "trimer of dimers" conformation for the hexamer that contains an unanticipated arrangement of conserved loops required for nucleic-acid translocation. RNA extends across a shallow intersubunit channel formed by conserved amino acids required for RNA-stimulated ATP hydrolysis and translocation and directly contacts a conserved lysine, just upstream of the catalytic GKT triad, in the phosphate-binding (P loop) motif of the ATP-binding pocket. The structure explains the molecular effects of numerous mutations and provides new insights into the links between substrate recognition, ATP turnover, and coordinated strand movement.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17081977}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17081977 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17081977}}
==About this Structure==
==About this Structure==
Line 26: Line 30:
[[Category: Atpase]]
[[Category: Atpase]]
[[Category: Translocase]]
[[Category: Translocase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 30 13:57:22 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 10:31:47 2008''

Revision as of 07:32, 29 July 2008

Image:2ht1.png

Template:STRUCTURE 2ht1

The closed ring structure of the Rho transcription termination factor in complex with nucleic acid in the motor domains

Template:ABSTRACT PUBMED 17081977

About this Structure

2HT1 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structural insights into RNA-dependent ring closure and ATPase activation by the Rho termination factor., Skordalakes E, Berger JM, Cell. 2006 Nov 3;127(3):553-64. PMID:17081977

Page seeded by OCA on Tue Jul 29 10:31:47 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2ht1"
Personal tools