3tfs | pdb_00003tfs
From Proteopedia
Ternary complex structure of DNA polymerase beta with a gapped DNA substrate and a, b dAMP(CFH)PP in the active site: Stereoselective binding of (S) isomer
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Structural highlights
Function[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.[1] [2] [3] [4] Publication Abstract from PubMedThe influence of water: Crystallization of (R/S)-alpha,beta-CHF-dATP with the preorganized pol beta-DNA complex shows that (S)-alpha,beta-CHF-dATP is preferentially bound to the active site with the CF fluorine proximal to a structural water bound to Asp276. Stereospecific Formation of a Ternary Complex of (S)-alpha,beta-Fluoromethylene-dATP with DNA Pol beta.,Chamberlain BT, Batra VK, Beard WA, Kadina AP, Shock DD, Kashemirov BA, McKenna CE, Goodman MF, Wilson SH Chembiochem. 2012 Mar 5;13(4):528-30. doi: 10.1002/cbic.201100738. Epub 2012 Feb , 7. PMID:22315190[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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