7ESQ

Structure and mutation analysis of the hexameric P4 from Pseudomonas aeruginosa phage phiYY

Summary for 7ESQ

• Entry DOI: 10.2210/pdb7esq/pdb
• Descriptor: Packaging NTPase, MAGNESIUM ION, PYROPHOSPHATE, ... (5 entities in total)
• Functional Keywords: cystoviruses, phiyy p4, ntpase, viral protein, hydrolase
• Biological source: Pseudomonas phage phiYY
• Total number of polymer chains: 2
• Total formula weight: 75506.10

Authors

Zhang, C.Y.,Jin, T.C. (deposition date: 2021-05-11, release date: 2022-03-23, Last modification date: 2023-11-29)

Primary citation

Zhang, C.,Li, Y.,Samad, A.,Zheng, P.,Ji, Z.,Chen, F.,Zhang, H.,Jin, T.
Structure and mutation analysis of the hexameric P4 from Pseudomonas aeruginosa phage phiYY.
Int.J.Biol.Macromol., 194:42-49, 2022

PubMed Abstract: phiYY is a foremost member of Cystoviridae isolated from Pseudomonas aeruginosa. Its P4 protein with NTPase activity is a molecular motor for their genome packing during viral particle assembly. Previously studies on the P4 from four Pseudomonas phages phi6, phi8, phi12 and phi13 reveal that despite of belonging to the same protein family, they are unique in sequence, structure and biochemical properties. To better understand the structure and function of phiYY P4, four crystal structures of phiYY P4 in apo-form or combined with different ligands were solved at the resolution between 1.85 Å and 2.43 Å, which showed drastic conformation change of the H1 motif in ligand-bound forms compared with in apo-form, a four residue-mutation at the ligand binding pocket abolished its ATPase activity. Furthermore, the truncation mutation of the 50 residues at the C-terminal did not impair the hexamerization and ATP hydrolysis.

PubMed: 34856215
DOI: 10.1016/j.ijbiomac.2021.11.129

Experimental method

X-RAY DIFFRACTION (1.85 Å)