2vhc

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2vhc.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2vhc.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2vhc| PDB=2vhc | SCENE= }}
{{STRUCTURE_2vhc| PDB=2vhc | SCENE= }}
-
'''P4 PROTEIN FROM BACTERIOPHAGE PHI12 N234G MUTANT IN COMPLEX WITH AMPCPP AND MN'''
+
===P4 PROTEIN FROM BACTERIOPHAGE PHI12 N234G MUTANT IN COMPLEX WITH AMPCPP AND MN===
-
==Overview==
+
<!--
-
The P4 protein of bacteriophage varphi12 is a hexameric molecular motor closely related to superfamily 4 helicases. P4 converts chemical energy from ATP hydrolysis into mechanical work, to translocate single-stranded RNA into a viral capsid. The molecular basis of mechanochemical coupling, i.e. how small approximately 1 A changes in the ATP-binding site are amplified into nanometer scale motion along the nucleic acid, is not understood at the atomic level. Here we study in atomic detail the mechanochemical coupling using structural and biochemical analyses of P4 mutants. We show that a conserved region, consisting of superfamily 4 helicase motifs H3 and H4 and loop L2, constitutes the moving lever of the motor. The lever tip encompasses an RNA-binding site that moves along the mechanical reaction coordinate. The lever is flanked by gamma-phosphate sensors (Asn-234 and Ser-252) that report the nucleotide state of neighboring subunits and control the lever position. Insertion of an arginine finger (Arg-279) into the neighboring catalytic site is concomitant with lever movement and commences ATP hydrolysis. This ensures cooperative sequential hydrolysis that is tightly coupled to mechanical motion. Given the structural conservation, the mutated residues may play similar roles in other hexameric helicases and related molecular motors.
+
The line below this paragraph, {{ABSTRACT_PUBMED_18057007}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 18057007 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_18057007}}
==About this Structure==
==About this Structure==
Line 36: Line 40:
[[Category: Packaging atpase]]
[[Category: Packaging atpase]]
[[Category: Virus dsrna]]
[[Category: Virus dsrna]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 18:48:29 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 16:51:10 2008''

Revision as of 13:51, 27 July 2008

Image:2vhc.png

Template:STRUCTURE 2vhc

P4 PROTEIN FROM BACTERIOPHAGE PHI12 N234G MUTANT IN COMPLEX WITH AMPCPP AND MN

Template:ABSTRACT PUBMED 18057007

About this Structure

2VHC is a Single protein structure of sequence from Pseudomonas phage phi12. Full crystallographic information is available from OCA.

Reference

Structural Basis of Mechanochemical Coupling in a Hexameric Molecular Motor., Kainov DE, Mancini EJ, Telenius J, Lisal J, Grimes JM, Bamford DH, Stuart DI, Tuma R, J Biol Chem. 2008 Feb 8;283(6):3607-3617. Epub 2007 Dec 5. PMID:18057007

Page seeded by OCA on Sun Jul 27 16:51:10 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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