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4blo
From Proteopedia
(Difference between revisions)
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===P4 PROTEIN FROM BACTERIOPHAGE PHI6 IN COMPLEX WITH ADP=== | ===P4 PROTEIN FROM BACTERIOPHAGE PHI6 IN COMPLEX WITH ADP=== | ||
{{ABSTRACT_PUBMED_23939620}} | {{ABSTRACT_PUBMED_23939620}} | ||
| + | |||
| + | ==Function== | ||
| + | [[http://www.uniprot.org/uniprot/P4_BPPH6 P4_BPPH6]] P4 is one of the structural proteins of the polyhedral procapsid, which is responsible for genomic replication and transcription. Displays single-stranded RNA-stimulated NTPase activity.<ref>PMID:12239286</ref> | ||
==About this Structure== | ==About this Structure== | ||
| - | [[4blo]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | [[4blo]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpph6 Bpph6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BLO OCA]. |
==Reference== | ==Reference== | ||
<ref group="xtra">PMID:023939620</ref><references group="xtra"/><references/> | <ref group="xtra">PMID:023939620</ref><references group="xtra"/><references/> | ||
| + | [[Category: Bpph6]] | ||
[[Category: Nucleoside-triphosphatase]] | [[Category: Nucleoside-triphosphatase]] | ||
| - | [[Category: Pseudomonas phage phi6]] | ||
[[Category: Bamford, D H.]] | [[Category: Bamford, D H.]] | ||
[[Category: Grimes, J M.]] | [[Category: Grimes, J M.]] | ||
Revision as of 06:25, 13 November 2013
Contents |
P4 PROTEIN FROM BACTERIOPHAGE PHI6 IN COMPLEX WITH ADP
Template:ABSTRACT PUBMED 23939620
Function
[P4_BPPH6] P4 is one of the structural proteins of the polyhedral procapsid, which is responsible for genomic replication and transcription. Displays single-stranded RNA-stimulated NTPase activity.[1]
About this Structure
4blo is a 12 chain structure with sequence from Bpph6. Full crystallographic information is available from OCA.
Reference
- El Omari K, Meier C, Kainov D, Sutton G, Grimes JM, Poranen MM, Bamford DH, Tuma R, Stuart DI, Mancini EJ. Tracking in atomic detail the functional specializations in viral RecA helicases that occur during evolution. Nucleic Acids Res. 2013 Aug 11. PMID:23939620 doi:10.1093/nar/gkt713
