4mff: Difference between revisions

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'''Unreleased structure'''
{{STRUCTURE_4mff|  PDB=4mff  |  SCENE=  }}
===Structure of human DNA polymerase beta complexed with O6MG in the template base paired with incoming non-hydrolyzable TTP===
{{ABSTRACT_PUBMED_24694247}}


The entry 4mff is ON HOLD until Paper Publication
==Function==
[[http://www.uniprot.org/uniprot/DPOLB_HUMAN DPOLB_HUMAN]] Repair polymerase that plays a key role in base-excision repair. Has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity that removes the 5' sugar phosphate and also acts as a DNA polymerase that adds one nucleotide to the 3' end of the arising single-nucleotide gap. Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases.<ref>PMID:9207062</ref> <ref>PMID:9572863</ref> <ref>PMID:11805079</ref> <ref>PMID:21362556</ref>  


Authors: Koag, M.C., Min, K., Monzingo, A.F., Lee, S.
==About this Structure==
[[4mff]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MFF OCA].  


Description: Structure of human DNA polymerase beta complexed with O6MG in the template base paired with incoming non-hydrolyzable TTP
==Reference==
<ref group="xtra">PMID:024694247</ref><references group="xtra"/><references/>
[[Category: Koag, M C.]]
[[Category: Lee, S.]]
[[Category: Min, K.]]
[[Category: Monzingo, A F.]]
[[Category: Dna polymerase x family]]
[[Category: Dna synthesis]]
[[Category: Transferase-dna complex]]