2rt6
From Proteopedia
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- | + | {{STRUCTURE_2rt6| PDB=2rt6 | SCENE= }} | |
+ | ===Backbone 1H, 13C, and 15N Chemical Shift Assignments for PriC N-terminal domain=== | ||
+ | {{ABSTRACT_PUBMED_23868391}} | ||
- | + | ==Function== | |
+ | [[http://www.uniprot.org/uniprot/PRIC_ECOLI PRIC_ECOLI]] PriA recognizes a specific hairpin sequence on bacteriophage phi X174 ssDNA. This structure is then recognized and bound by proteins PriB and PriC. Formation of the primosome proceeds with the subsequent actions of DnaB, DnaC, DnaT and primase. | ||
- | + | ==About this Structure== | |
+ | [[2rt6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RT6 OCA]. | ||
- | + | ==Reference== | |
+ | <ref group="xtra">PMID:023868391</ref><references group="xtra"/><references/> | ||
+ | [[Category: Escherichia coli k-12]] | ||
+ | [[Category: Abe, Y.]] | ||
+ | [[Category: Aramaki, T.]] | ||
+ | [[Category: Katayama, T.]] | ||
+ | [[Category: Ueda, T.]] | ||
+ | [[Category: Dna binding protein]] | ||
+ | [[Category: Pric]] | ||
+ | [[Category: Primosome]] | ||
+ | [[Category: Replication restart]] |
Revision as of 20:56, 7 August 2013
Contents |
Backbone 1H, 13C, and 15N Chemical Shift Assignments for PriC N-terminal domain
Template:ABSTRACT PUBMED 23868391
Function
[PRIC_ECOLI] PriA recognizes a specific hairpin sequence on bacteriophage phi X174 ssDNA. This structure is then recognized and bound by proteins PriB and PriC. Formation of the primosome proceeds with the subsequent actions of DnaB, DnaC, DnaT and primase.
About this Structure
2rt6 is a 1 chain structure with sequence from Escherichia coli k-12. Full experimental information is available from OCA.
Reference
- Aramaki T, Abe Y, Katayama T, Ueda T. Solution structure of the N-terminal domain of a replication restart primosome factor, PriC, in Escherichia coli. Protein Sci. 2013 Jul 19. doi: 10.1002/pro.2314. PMID:23868391 doi:10.1002/pro.2314