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Literature summary for 3.1.99.B1 extracted from

  • Tsutakawa, S.E.; Classen, S.; Chapados, B.R.; Arvai, A.S.; Finger, L.D.; Guenther, G.; Tomlinson, C.G.; Thompson, P.; Sarker, A.H.; Shen, B.; Cooper, P.K.; Grasby, J.A.; Tainer, J.A.
    Human flap endonuclease structures, DNA double-base flipping, and a unified understanding of the FEN1 superfamily (2011), Cell, 145, 198-211.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.99.B1

Cloned(Commentary)

Cloned (Comment) Organism
expression of His6-tagged FEN1 mutant DELTA 336 and FEN1 mutant DELTA 336 D181A in Escherichia coli Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant His-tagged FEN1 mutant DELTA 336 and FEN1 mutant DELTA 336 D181A, X-ray diffraction structure determination and analysis Homo sapiens

Protein Variants

Protein Variants Comment Organism
D181A construction of a FEN1 mutant DELTA 336 truncated after residue 336 that bears an additional point mutation at residue 181. FEN1 DELTA336 removes only the flexible, protruding PCNA binding motif and encompasses the entire catalytic domain, and the active site D181A mutation severely retards incision. The DNA contains competing base pairing purine-pyrimidine pairs at the DNA junction, but the C-A mismatch favors 1 nt 3' flap formation Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ two Sm3+ ions occupy Mg2+ ion sites seen in the FEN1 DNA-free structure Homo sapiens
Sm3+ in the active site, the 5'-monophosphate of the cleaved product nt (-1) is coordinated by two Sm3+ ions. Sm1 is coordinated by Asp86, Glu160, and two oxygens of the cleaved 5'-monophosphate. Sm2 is coordinated by Glu160, Asp179, Asp181 and one phosphate oxygen. Asp34, Glu158, and Asp233 interact with Sm3+ via waters Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens FEN1 contacts the DNA primarily with helix and loop elements. Most interactions are to template strand and terminal flap nts. FEN1 with metal ions has a 1828 A2 interface with product DNA, substrate and product binding structures, detailed overview ?
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Organism

Organism UniProt Comment Textmining
Homo sapiens
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Purification (Commentary)

Purification (Comment) Organism
recombinant His6-tagged FEN1 mutant DELTA 336 and FEN1 mutant DELTA 336 D181A from Escherichia coli Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information FEN1 contacts the DNA primarily with helix and loop elements. Most interactions are to template strand and terminal flap nts. FEN1 with metal ions has a 1828 A2 interface with product DNA, substrate and product binding structures, detailed overview Homo sapiens ?
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 ?

Synonyms

Synonyms Comment Organism
FEN1
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 Homo sapiens
flap endonuclease 1
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 Homo sapiens
More the enzyme belongs to the FEN1 superfamily Homo sapiens