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2o0k

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Revision as of 08:46, 18 October 2017

T4 gp17 ATPase domain mutant

Structural highlights

2o0k is a 1 chain structure with sequence from Bpt4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	2o0h, 2o0j
Gene:	17 (BPT4)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[TERL_BPT4] Component of the molecular motor that translocates genomic DNA in empty capsid during DNA packaging. Heterodimerizes with small terminase protein to be docked on capsid portal protein. The latter forms a ring in which genomic DNA in translocated into the capsid. May have or induce an endonuclease activity to cleave the genome concatemer after encapsidation (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Packaging the viral genome into empty procapsids, an essential event in the life cycle of tailed bacteriophages and some eukaryotic viruses, is a process that shares features with chromosome assembly. Most viral procapsids possess a special vertex containing a dodecameric portal protein that is used for entry and exit of the viral genome. The portal and an ATPase are parts of the genome-packaging machine. The ATPase is required to provide energy for translocation and compaction of the negative charges on the genomic DNA. Here we report the atomic structure of the ATPase component in a phage DNA-packaging machine. The bacteriophage T4 ATPase has the greatest similarity to monomeric helicases, suggesting that the genome is translocated by an inchworm mechanism. The similarity of the packaging machines in the double-stranded DNA (dsDNA) bacteriophage T4 and dsRNA bacteriophage varphi12 is consistent with the evolution of many virions from a common ancestor.

The structure of the ATPase that powers DNA packaging into bacteriophage T4 procapsids.,Sun S, Kondabagil K, Gentz PM, Rossmann MG, Rao VB Mol Cell. 2007 Mar 23;25(6):943-9. PMID:17386269^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Sun S, Kondabagil K, Gentz PM, Rossmann MG, Rao VB. The structure of the ATPase that powers DNA packaging into bacteriophage T4 procapsids. Mol Cell. 2007 Mar 23;25(6):943-9. PMID:17386269 doi:10.1016/j.molcel.2007.02.013

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2o0k"

Categories: Bpt4 | Rossmann, M G | Sun, S | Hydrolase | Nucleotide-binding fold

@@ Line 1: / Line 1: @@
 ==T4 gp17 ATPase domain mutant==
 <StructureSection load='2o0k' size='340' side='right' caption='[[2o0k]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2o0h|2o0h]], [[2o0j|2o0j]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">17 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10665 BPT4])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2o0k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o0k OCA], [http://pdbe.org/2o0k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2o0k RCSB], [http://www.ebi.ac.uk/pdbsum/2o0k PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2o0k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o0k OCA], [http://pdbe.org/2o0k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2o0k RCSB], [http://www.ebi.ac.uk/pdbsum/2o0k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2o0k ProSAT]</span></td></tr>
 </table>
 == Function ==

2o0k

From Proteopedia

Revision as of 08:46, 18 October 2017

T4 gp17 ATPase domain mutant

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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