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{{STRUCTURE_4lim| PDB=4lim | SCENE= }} | |||
===Crystal structure of the catalytic subunit of yeast primase=== | |||
{{ABSTRACT_PUBMED_24239947}} | |||
==Function== | |||
[[http://www.uniprot.org/uniprot/PRI1_YEAST PRI1_YEAST]] DNA primase is the polymerase that synthesizes small RNA primers for the Okazaki fragments made during discontinuous DNA replication. In a complex with DNA polymerase alpha (DNA polymerase alpha:primase) constitutes a replicative polymerase. Both primase components participate in formation of the active center, but the ATP-binding site is exclusively located on p48. | |||
==About this Structure== | |||
[[4lim]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LIM OCA]. | |||
==Reference== | |||
<ref group="xtra">PMID:024239947</ref><references group="xtra"/><references/> | |||
[[Category: Berger, J M.]] | |||
[[Category: Chazin, W J.]] | |||
[[Category: Corn, J.]] | |||
[[Category: Stephenson, S.]] | |||
[[Category: Vaithiyalingam, S.]] | |||
[[Category: Prim fold]] | |||
[[Category: Transferase]] |
Revision as of 13:23, 18 December 2013
Crystal structure of the catalytic subunit of yeast primaseCrystal structure of the catalytic subunit of yeast primase
Template:ABSTRACT PUBMED 24239947
FunctionFunction
[PRI1_YEAST] DNA primase is the polymerase that synthesizes small RNA primers for the Okazaki fragments made during discontinuous DNA replication. In a complex with DNA polymerase alpha (DNA polymerase alpha:primase) constitutes a replicative polymerase. Both primase components participate in formation of the active center, but the ATP-binding site is exclusively located on p48.
About this StructureAbout this Structure
4lim is a 1 chain structure. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ Vaithiyalingam S, Arnett DR, Aggarwal A, Eichman BF, Fanning E, Chazin WJ. Insights into Eukaryotic Primer Synthesis from Structures of the p48 Subunit of Human DNA Primase. J Mol Biol. 2013 Nov 13. pii: S0022-2836(13)00718-3. doi:, 10.1016/j.jmb.2013.11.007. PMID:24239947 doi:http://dx.doi.org/10.1016/j.jmb.2013.11.007