5oe8: Difference between revisions
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<StructureSection load='5oe8' size='340' side='right'caption='[[5oe8]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='5oe8' size='340' side='right'caption='[[5oe8]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5oe8]] is a 3 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5oe8]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Deep-sea_thermophilic_phage_D6E Deep-sea thermophilic phage D6E]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OE8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OE8 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5oe8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oe8 OCA], [https://pdbe.org/5oe8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5oe8 RCSB], [https://www.ebi.ac.uk/pdbsum/5oe8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5oe8 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/E5DV50_9CAUD E5DV50_9CAUD] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[Terminase|Terminase]] | *[[Terminase 3D Structures|Terminase 3D Structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Deep-sea thermophilic | [[Category: Deep-sea thermophilic phage D6E]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Antson | [[Category: Antson AA]] | ||
[[Category: Greive | [[Category: Greive SJ]] | ||
[[Category: Jenkins | [[Category: Jenkins HT]] | ||
[[Category: Xu | [[Category: Xu RG]] | ||
Latest revision as of 19:46, 13 December 2023
Structure of large terminase from the thermophilic bacteriophage D6E (Crystal form 2)Structure of large terminase from the thermophilic bacteriophage D6E (Crystal form 2)
Structural highlights
FunctionPublication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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