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Literature summary for 5.6.2.3 extracted from

  • Wu, Y.; Brosh, R.M.
    DNA helicase and helicase-nuclease enzymes with a conserved iron-sulfur cluster (2012), Nucleic Acids Res., 40, 4247-4260.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Sulfolobus acidocaldarius
expressed in Escherichia coli Thermoplasma acidophilum

Crystallization (Commentary)

Crystallization (Comment) Organism
all solved XPD structures contain two Rad51/RecQ-like domains (HD1 and HD2) with two additional domains, the Fe-S and Arch domains, inserted between adjacent beta-strands of the central beta-sheet of HD1 Sulfolobus acidocaldarius
crystal structure in complex with a short DNA fragment is reported Thermoplasma acidophilum

Protein Variants

Protein Variants Comment Organism
additional information mutations of the Fe-S domain, including the conserved cysteines, abolishes SaXPD helicase activity and destabilizes tertiary structure, attesting to the structural importance of the Fe-S domain Sulfolobus acidocaldarius
additional information site-directed mutagenesis of the four conserved cysteines of the Fe-S cluster in the Rad3 (XPD) helicase from Ferroplasma acidarmanus (FacXPD) revealed that the integrity of the domain is required for the proper folding and structural stability of the auxiliary domain and is important for coupling ATP hydrolysis to unidirectional translocation of helicase Ferroplasma acidarmanus
R112H most common mutations in TTD patients, amino acid substitution R112H, is localized in the Fe-S domain of XPD just before the first conserved cysteine residue. Missense mutation results in a complete loss of XPD helicase activity and a reduced basal transcription activity of the TFIIH complex Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Fe-S
-
Homo sapiens
Fe-S
-
Thermoplasma acidophilum
Fe-S
-
Ferroplasma acidarmanus
Fe-S Fe-S domain is not essential for SaXPD protein stability, the enzyme's ability to bind to single-stranded DNA, or its ATPase activity, but is required for helicase activity Sulfolobus acidocaldarius

Organism

Organism UniProt Comment Textmining
Ferroplasma acidarmanus
-
-
-
Homo sapiens
-
-
-
Sulfolobus acidocaldarius
-
-
-
Thermoplasma acidophilum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Sulfolobus acidocaldarius
-
Thermoplasma acidophilum

Synonyms

Synonyms Comment Organism
FacXPD
-
Ferroplasma acidarmanus
SaXPD
-
Sulfolobus acidocaldarius
taXPD
-
Thermoplasma acidophilum
XPD
-
Homo sapiens