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PDBsum entry 5oeb
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Viral protein
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PDB id
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5oeb
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References listed in PDB file
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Key reference
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Title
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Structure of the large terminase from a hyperthermophilic virus reveals a unique mechanism for oligomerization and ATP hydrolysis.
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Authors
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R.G.Xu,
H.T.Jenkins,
A.A.Antson,
S.J.Greive.
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Ref.
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Nucleic Acids Res, 2017,
45,
13029-13042.
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PubMed id
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Abstract
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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.
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