1w4c
From Proteopedia
(New page: 200px<br /><applet load="1w4c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1w4c, resolution 2.5Å" /> '''P4 PROTEIN FROM BACTE...) |
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| - | [[Image:1w4c.gif|left|200px]]<br /><applet load="1w4c" size=" | + | [[Image:1w4c.gif|left|200px]]<br /><applet load="1w4c" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1w4c, resolution 2.5Å" /> | caption="1w4c, resolution 2.5Å" /> | ||
'''P4 PROTEIN FROM BACTERIOPHAGE PHI12 APO STATE'''<br /> | '''P4 PROTEIN FROM BACTERIOPHAGE PHI12 APO STATE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Many viruses package their genome into preformed capsids using packaging | + | Many viruses package their genome into preformed capsids using packaging motors powered by the hydrolysis of ATP. The hexameric ATPase P4 of dsRNA bacteriophage phi12, located at the vertices of the icosahedral capsid, is such a packaging motor. We have captured crystallographic structures of P4 for all the key points along the catalytic pathway, including apo, substrate analog bound, and product bound. Substrate and product binding have been observed as both binary complexes and ternary complexes with divalent cations. These structures reveal large movements of the putative RNA binding loop, which are coupled with nucleotide binding and hydrolysis, indicating how ATP hydrolysis drives RNA translocation through cooperative conformational changes. Two distinct conformations of bound nucleotide triphosphate suggest how hydrolysis is activated by RNA binding. This provides a model for chemomechanical coupling for a prototype of the large family of hexameric helicases and oligonucleotide translocating enzymes. |
==About this Structure== | ==About this Structure== | ||
| - | 1W4C 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]. Full crystallographic information is available from [http:// | + | 1W4C 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]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W4C OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Pseudomonas phage phi6]] | [[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: Mancini, E | + | [[Category: Mancini, E J.]] |
| - | [[Category: Stuart, D | + | [[Category: Stuart, D I.]] |
[[Category: Tuma, R.]] | [[Category: Tuma, R.]] | ||
[[Category: dsrna virus]] | [[Category: dsrna virus]] | ||
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[[Category: packaging atpase]] | [[Category: packaging atpase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:40:23 2008'' |
Revision as of 13:40, 21 February 2008
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P4 PROTEIN FROM BACTERIOPHAGE PHI12 APO STATE
Overview
Many viruses package their genome into preformed capsids using packaging motors powered by the hydrolysis of ATP. The hexameric ATPase P4 of dsRNA bacteriophage phi12, located at the vertices of the icosahedral capsid, is such a packaging motor. We have captured crystallographic structures of P4 for all the key points along the catalytic pathway, including apo, substrate analog bound, and product bound. Substrate and product binding have been observed as both binary complexes and ternary complexes with divalent cations. These structures reveal large movements of the putative RNA binding loop, which are coupled with nucleotide binding and hydrolysis, indicating how ATP hydrolysis drives RNA translocation through cooperative conformational changes. Two distinct conformations of bound nucleotide triphosphate suggest how hydrolysis is activated by RNA binding. This provides a model for chemomechanical coupling for a prototype of the large family of hexameric helicases and oligonucleotide translocating enzymes.
About this Structure
1W4C is a Single protein structure of sequence from Pseudomonas phage phi6. Full crystallographic information is available from OCA.
Reference
Atomic snapshots of an RNA packaging motor reveal conformational changes linking ATP hydrolysis to RNA translocation., Mancini EJ, Kainov DE, Grimes JM, Tuma R, Bamford DH, Stuart DI, Cell. 2004 Sep 17;118(6):743-55. PMID:15369673
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