5oea

Structure of large terminase from the thermophilic bacteriophage D6E in complex with ATP-gamma-S (Crystal form 3)

spinqualitylabelsall models 5oea, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5oea is a 6 chain structure with sequence from Deep-sea thermophilic phage D6E. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3Å Ligands: AGS, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function E5DV50_9CAUD Publication Abstract from PubMed 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 k cat 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. Structure of the large terminase from a hyperthermophilic virus reveals a unique mechanism for oligomerization and ATP hydrolysis.,Xu RG, Jenkins HT, Antson AA, Greive SJ Nucleic Acids Res. 2017 Oct 24. pii: 4563303. doi: 10.1093/nar/gkx947. PMID:29069443 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Terminase 3D Structures

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