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| [[Image:1w47.gif|left|200px]] | | {{Seed}} |
| | [[Image:1w47.png|left|200px]] |
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| {{STRUCTURE_1w47| PDB=1w47 | SCENE= }} | | {{STRUCTURE_1w47| PDB=1w47 | SCENE= }} |
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| '''P4 PROTEIN FROM BACTERIOPHAGE PHI12 IN COMPLEX WITH ADP AND MN'''
| | ===P4 PROTEIN FROM BACTERIOPHAGE PHI12 IN COMPLEX WITH ADP AND MN=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_15369673}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15369673 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15369673}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Non-hydrolysable atp analogue]] | | [[Category: Non-hydrolysable atp analogue]] |
| [[Category: Packaging atpase]] | | [[Category: Packaging atpase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:08:00 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:38:52 2008'' |