2vhc
From Proteopedia
(New page: 200px<br /><applet load="2vhc" size="350" color="white" frame="true" align="right" spinBox="true" caption="2vhc, resolution 2.35Å" /> '''P4 PROTEIN FROM BACT...) |
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caption="2vhc, resolution 2.35Å" /> | caption="2vhc, resolution 2.35Å" /> | ||
'''P4 PROTEIN FROM BACTERIOPHAGE PHI12 N234G MUTANT IN COMPLEX WITH AMPCPP AND MN'''<br /> | '''P4 PROTEIN FROM BACTERIOPHAGE PHI12 N234G MUTANT IN COMPLEX WITH AMPCPP AND MN'''<br /> | ||
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| + | ==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. | ||
==About this Structure== | ==About this Structure== | ||
| - | 2VHC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ | + | 2VHC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_phage_phi6 Pseudomonas phage phi6] with <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=APC:'>APC</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=AC1:Apc+Binding+Site+For+Chain+A'>AC1</scene>, <scene name='pdbsite=AC2:Mn+Binding+Site+For+Chain+A'>AC2</scene>, <scene name='pdbsite=AC3:Apc+Binding+Site+For+Chain+B'>AC3</scene>, <scene name='pdbsite=AC4:Mn+Binding+Site+For+Chain+B'>AC4</scene>, <scene name='pdbsite=AC5:Apc+Binding+Site+For+Chain+C'>AC5</scene> and <scene name='pdbsite=AC6:Mn+Binding+Site+For+Chain+C'>AC6</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VHC OCA]. |
| - | [[Category: Pseudomonas phage | + | |
| + | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18057007 18057007] | ||
| + | [[Category: Pseudomonas phage phi6]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bamford, D | + | [[Category: Bamford, D H.]] |
| - | [[Category: Grimes, J | + | [[Category: Grimes, J M.]] |
| - | [[Category: Kainov, D | + | [[Category: Kainov, D E.]] |
[[Category: Lisal, J.]] | [[Category: Lisal, J.]] | ||
| - | [[Category: Mancini, E | + | [[Category: Mancini, E J.]] |
| - | [[Category: Stuart, D | + | [[Category: Stuart, D I.]] |
[[Category: Telenius, J.]] | [[Category: Telenius, J.]] | ||
[[Category: Tuma, R.]] | [[Category: Tuma, R.]] | ||
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[[Category: virus dsrna]] | [[Category: virus dsrna]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:55:59 2008'' |
Revision as of 16:56, 21 February 2008
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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.
About this Structure
2VHC is a Single protein structure of sequence from Pseudomonas phage phi6 with and as ligands. Known structural/functional Sites: , , , , and . 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
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