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.


2gxu

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2gxu.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2gxu.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2gxu| PDB=2gxu | SCENE= }}
{{STRUCTURE_2gxu| PDB=2gxu | SCENE= }}
-
'''HERA N-terminal domain in complex with orthophosphate, crystal form 1'''
+
===HERA N-terminal domain in complex with orthophosphate, crystal form 1===
-
==Overview==
+
<!--
-
DEAD box RNA helicases use the energy of ATP hydrolysis to unwind double-stranded RNA regions or to disrupt RNA/protein complexes. A minimal RNA helicase comprises nine conserved motifs distributed over two RecA-like domains. The N-terminal domain contains all motifs involved in nucleotide binding, namely the Q-motif, the DEAD box, and the P-loop, as well as the SAT motif, which has been implicated in the coordination of ATP hydrolysis and RNA unwinding. We present here the crystal structure of the N-terminal domain of the Thermus thermophilus RNA helicase Hera in complex with adenosine monophosphate (AMP). Upon binding of AMP the P-loop adopts a partially collapsed or half-open conformation that is still connected to the DEAD box motif, and the DEAD box in turn is linked to the SAT motif via hydrogen bonds. This network of interactions communicates changes in the P-loop conformation to distant parts of the helicase. The affinity of AMP is comparable to that of ADP and ATP, substantiating that the binding energy from additional phosphate moieties is directly converted into conformational changes of the entire helicase. Importantly, the N-terminal Hera domain forms a dimer in the crystal similar to that seen in another thermophilic prokaryote. It is possible that this mode of dimerization represents the prototypic architecture in RNA helicases of thermophilic origin.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16890241}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16890241 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16890241}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Rna helicase]]
[[Category: Rna helicase]]
[[Category: Thermophilic]]
[[Category: Thermophilic]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:39:00 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:43:42 2008''

Revision as of 03:43, 29 July 2008

Image:2gxu.png

Template:STRUCTURE 2gxu

HERA N-terminal domain in complex with orthophosphate, crystal form 1

Template:ABSTRACT PUBMED 16890241

About this Structure

2GXU is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.

Reference

Crystal structure and nucleotide binding of the Thermus thermophilus RNA helicase Hera N-terminal domain., Rudolph MG, Heissmann R, Wittmann JG, Klostermeier D, J Mol Biol. 2006 Aug 25;361(4):731-43. Epub 2006 Jul 12. PMID:16890241

Page seeded by OCA on Tue Jul 29 06:43:42 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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