1W44

P4 protein from Bacteriophage PHI12 in complex with ADP

Summary for 1W44

• Entry DOI: 10.2210/pdb1w44/pdb
• Descriptor: NTPASE P4, ADENOSINE-5'-DIPHOSPHATE (3 entities in total)
• Functional Keywords: virus dsrna, packaging atpase, hexameric helicase, molecular motor, non-hydrolysable atp analogue, hydrolase
• Biological source: BACTERIOPHAGE PHI-12 (BACTERIOPHAGE PHI12)
• Total number of polymer chains: 3
• Total formula weight: 106732.89

Authors

Mancini, E.J.,Kainov, D.E.,Grimes, J.M.,Tuma, R.,Bamford, D.H.,Stuart, D.I. (deposition date: 2004-07-22, release date: 2004-10-29, Last modification date: 2024-05-08)

Primary citation

Mancini, E.J.,Kainov, D.E.,Grimes, J.M.,Tuma, R.,Bamford, D.H.,Stuart, D.I.
Atomic Snapshots of an RNA Packaging Motor Reveal Conformational Changes Linking ATP Hydrolysis to RNA Translocation
Cell(Cambridge,Mass.), 118:743-, 2004

PubMed Abstract: 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.

PubMed: 15369673
DOI: 10.1016/J.CELL.2004.09.007

Experimental method

X-RAY DIFFRACTION (2 Å)