5OE9

Structure of large terminase from the thermophilic bacteriophage D6E in complex with sulfate (Crystal form 2)

Summary for 5OE9

• Entry DOI: 10.2210/pdb5oe9/pdb
• Related: 5OE8
• Descriptor: Large subunit terminase, SULFATE ION (3 entities in total)
• Functional Keywords: large terminase, viral protein
• Biological source: Deep-sea thermophilic phage D6E
• Total number of polymer chains: 3
• Total formula weight: 150979.79

Authors

Xu, R.G.,Jenkins, H.T.,Greive, S.J.,Antson, A.A. (deposition date: 2017-07-07, release date: 2017-10-11, Last modification date: 2024-05-08)

Primary citation

Xu, R.G.,Jenkins, H.T.,Antson, A.A.,Greive, S.J.
Structure of the large terminase from a hyperthermophilic virus reveals a unique mechanism for oligomerization and ATP hydrolysis.
Nucleic Acids Res., 45:13029-13042, 2017

PubMed Abstract: The crystal structure of the large terminase from the Geobacillus stearothermophilus bacteriophage D6E shows a unique relative orientation of the N-terminal adenosine triphosphatase (ATPase) and C-terminal nuclease domains. This monomeric 'initiation' state with the two domains 'locked' together is stabilized via a conserved C-terminal arm, which may interact with the portal protein during motor assembly, as predicted for several bacteriophages. Further work supports the formation of an active oligomeric state: (i) AUC data demonstrate the presence of oligomers; (ii) mutational analysis reveals a trans-arginine finger, R158, indispensable for ATP hydrolysis; (iii) the location of this arginine is conserved with the HerA/FtsK ATPase superfamily; (iv) a molecular docking model of the pentamer is compatible with the location of the identified arginine finger. However, this pentameric model is structurally incompatible with the monomeric 'initiation' state and is supported by the observed increase in kcat of ATP hydrolysis, from 7.8 ± 0.1 min-1 to 457.7 ± 9.2 min-1 upon removal of the C-terminal nuclease domain. Taken together, these structural, biophysical and biochemical data suggest a model where transition from the 'initiation' state into a catalytically competent pentameric state, is accompanied by substantial domain rearrangements, triggered by the removal of the C-terminal arm from the ATPase active site.

PubMed: 29069443
DOI: 10.1093/nar/gkx947

Experimental method

X-RAY DIFFRACTION (2.4 Å)