4khs: Difference between revisions
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{{STRUCTURE_4khs| PDB=4khs | SCENE= }} | {{STRUCTURE_4khs| PDB=4khs | SCENE= }} | ||
===Ternary complex of RB69 mutant L415F with a ribonucleotide at 0 position=== | ===Ternary complex of RB69 mutant L415F with a ribonucleotide at 0 position=== | ||
{{ABSTRACT_PUBMED_24082122}} | |||
==Function== | ==Function== | ||
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==About this Structure== | ==About this Structure== | ||
[[4khs]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_rb69 Enterobacteria phage rb69]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KHS OCA]. | [[4khs]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_rb69 Enterobacteria phage rb69]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KHS OCA]. | ||
==Reference== | |||
<ref group="xtra">PMID:024082122</ref><references group="xtra"/><references/> | |||
[[Category: DNA-directed DNA polymerase]] | [[Category: DNA-directed DNA polymerase]] | ||
[[Category: Enterobacteria phage rb69]] | [[Category: Enterobacteria phage rb69]] | ||
Revision as of 11:39, 30 October 2013
Ternary complex of RB69 mutant L415F with a ribonucleotide at 0 positionTernary complex of RB69 mutant L415F with a ribonucleotide at 0 position
Template:ABSTRACT PUBMED 24082122
FunctionFunction
[DPOL_BPR69] This polymerase possesses two enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic activity that degrades single stranded DNA in the 3'- to 5'-direction.
About this StructureAbout this Structure
4khs is a 3 chain structure with sequence from Enterobacteria phage rb69. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ Clausen AR, Murray MS, Passer AR, Pedersen LC, Kunkel TA. Structure-function analysis of ribonucleotide bypass by B family DNA replicases. Proc Natl Acad Sci U S A. 2013 Oct 15;110(42):16802-7. doi:, 10.1073/pnas.1309119110. Epub 2013 Sep 30. PMID:24082122 doi:http://dx.doi.org/10.1073/pnas.1309119110