4k3m
From Proteopedia
(Difference between revisions)
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{{STRUCTURE_4k3m| PDB=4k3m | SCENE= }} | {{STRUCTURE_4k3m| PDB=4k3m | SCENE= }} | ||
===E.coli sliding clamp in complex with AcALDLF peptide=== | ===E.coli sliding clamp in complex with AcALDLF peptide=== | ||
+ | {{ABSTRACT_PUBMED_24090409}} | ||
==Function== | ==Function== | ||
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==About this Structure== | ==About this Structure== | ||
- | [[4k3m]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | [[4k3m]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K3M OCA]. |
+ | |||
+ | ==Reference== | ||
+ | <ref group="xtra">PMID:024090409</ref><references group="xtra"/><references/> | ||
[[Category: DNA-directed DNA polymerase]] | [[Category: DNA-directed DNA polymerase]] | ||
- | [[Category: | + | [[Category: Ecoli]] |
[[Category: Oakley, A J.]] | [[Category: Oakley, A J.]] | ||
[[Category: Yin, Z.]] | [[Category: Yin, Z.]] | ||
[[Category: E. coli sliding clamp]] | [[Category: E. coli sliding clamp]] | ||
[[Category: Transferase]] | [[Category: Transferase]] |
Revision as of 07:17, 15 January 2014
Contents |
E.coli sliding clamp in complex with AcALDLF peptide
Template:ABSTRACT PUBMED 24090409
Function
[DPO3B_ECOLI] DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. The beta chain is required for initiation of replication once it is clamped onto DNA, it slides freely (bidirectional and ATP-independent) along duplex DNA.
About this Structure
4k3m is a 3 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA.
Reference
- Yin Z, Kelso MJ, Beck JL, Oakley AJ. Structural and Thermodynamic Dissection of Linear Motif Recognition by the E. coli Sliding Clamp. J Med Chem. 2013 Nov 14;56(21):8665-73. doi: 10.1021/jm401118f. Epub 2013 Oct 22. PMID:24090409 doi:http://dx.doi.org/10.1021/jm401118f