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Literature summary for 2.7.7.7 extracted from

  • Mukherjee, P.; Wilson, R.C.; Lahiri, I.; Pata, J.D.
    Three residues of the interdomain linker determine the conformation and single-base deletion fidelity of Y-family translesion polymerases (2014), J. Biol. Chem., 289, 6323-6331.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
crystals of mutant enzyme K242R/I243K/P244S are grown at room temperature by hanging-drop vapor diffusion, 2.4 A resolution crystal structure Sulfolobus acidocaldarius

Protein Variants

Protein Variants Comment Organism
K242R/I243K/P244S mutation of three linker amino acids, polymerase Dbh adopts the standard conformation of polymerase Dpo4. The interdomain linker also affects the single-base deletion frequency and the mispair extension efficiency of these polymerase Sulfolobus acidocaldarius

Organism

Organism UniProt Comment Textmining
Sulfolobus acidocaldarius Q4JB80
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Sulfolobus acidocaldarius DSM 639 Q4JB80
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Synonyms

Synonyms Comment Organism
DBH
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Sulfolobus acidocaldarius
Saci_0554 locus name Sulfolobus acidocaldarius