1w4b
P4 protein from PHI12 in complex with product (AMPcPP Mg 22C)P4 protein from PHI12 in complex with product (AMPcPP Mg 22C)
Structural highlights
FunctionPublication Abstract from PubMedMany 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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