8dgc

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Avs3 bound to phage PhiV-1 terminase

Structural highlights

8dgc is a 8 chain structure with sequence from Escherichia phage PhiV-1 and Salmonella enterica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 3.4Å
Ligands:ATP, MG
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

A0A7G3WWS0_9CAUD The terminase large subunit acts as an ATP driven molecular motor necessary for viral DNA translocation into empty capsids and as an endonuclease that cuts the viral genome at a unique and precise dsDNA sequence to initiate and to end a packaging reaction. The terminase lies at a unique vertex of the procapsid and is composed of two subunits, a small terminase subunit involved in viral DNA recognition (packaging sequence), and a large terminase subunit possessing endonucleolytic and ATPase activities. Both terminase subunits heterooligomerize and are docked on the portal protein to form the packaging machine. The terminase large subunit exhibits endonuclease activity and cleaves the viral genome concatemer. Once the DNA is packaged, the terminase detaches from the portal and gets replaced by the tail to finish maturation of the virion.[HAMAP-Rule:MF_04147]

See Also

Contents


PDB ID 8dgc

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OCA

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