4ezp: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| Line 8: | Line 8: | ||
==About this Structure== | ==About this Structure== | ||
[[4ezp]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EZP OCA]. | [[4ezp]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EZP OCA]. | ||
==Reference== | |||
<ref group="xtra">PMID:023562829</ref><references group="xtra"/><references/> | |||
[[Category: Escherichia coli k-12]] | [[Category: Escherichia coli k-12]] | ||
[[Category: Straeter, N.]] | [[Category: Straeter, N.]] | ||
Revision as of 07:32, 18 July 2013
Crystal structure of the substrate binding domain of E.coli DnaK in complex with A3-APO(residues 1 to 20)Crystal structure of the substrate binding domain of E.coli DnaK in complex with A3-APO(residues 1 to 20)
Template:ABSTRACT PUBMED 23562829
FunctionFunction
[DNAK_ECOLI] Plays an essential role in the initiation of phage lambda DNA replication, where it acts in an ATP-dependent fashion with the DnaJ protein to release lambda O and P proteins from the preprimosomal complex. DnaK is also involved in chromosomal DNA replication, possibly through an analogous interaction with the DnaA protein. Also participates actively in the response to hyperosmotic shock.[HAMAP-Rule:MF_00332]
About this StructureAbout this Structure
4ezp is a 4 chain structure with sequence from Escherichia coli k-12. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ Zahn M, Berthold N, Kieslich B, Knappe D, Hoffmann R, Strater N. Structural Studies on the Forward and Reverse Binding Modes of Peptides to the Chaperone DnaK. J Mol Biol. 2013 Apr 2. pii: S0022-2836(13)00208-8. doi:, 10.1016/j.jmb.2013.03.041. PMID:23562829 doi:10.1016/j.jmb.2013.03.041