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Literature summary 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)

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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.6.2.3 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
5.6.2.3 crystal structure in complex with a short DNA fragment is reported Thermoplasma acidophilum

Protein Variants

EC Number Protein Variants Comment Organism
5.6.2.3 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
5.6.2.3 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
5.6.2.3 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

EC Number Metals/Ions Comment Organism Structure
5.6.2.3 Fe-S
-
 Homo sapiens
5.6.2.3 Fe-S
-
 Thermoplasma acidophilum
5.6.2.3 Fe-S
-
 Ferroplasma acidarmanus
5.6.2.3 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

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

Purification (Commentary)

EC Number Purification (Comment) Organism
5.6.2.3
-
 Sulfolobus acidocaldarius
5.6.2.3
-
 Thermoplasma acidophilum

Synonyms

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