Literature summary for 5.6.1.1 extracted from

Taylor, J.; White, S.; Lauring, B.; Kull, F.
Crystal structure of the human spastin AAA domain (2012), J. Struct. Biol., 179, 133-137.

Search for more literature for 5.6.1.1

Cloned(Commentary)

Cloned (Comment)	Organism
GST fusion of amino acid residues 228-616 containing the E442Q mutation (42500 Da for the 389 amino acid residues construct (amino acid residues 228-616)), expressed in Escherichia coli BL21-CodonPlus (DE3)-RIPL	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging drop method, the N-terminal residues (about 10000 Da) are clipped off during time of crystal formation (5-7 days)	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
E442Q	residue of Walker B motif, hydrolysis deficient mutant, amino acid residues 228-616	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
GSTrap column chromatography, GST tag cleaved with PreScission Protease, GST-Sepharose chromatography, gel filtration	Homo sapiens

Subunits

Subunits	Comment	Organism
hexamer	full length protein, hexameric ring, sedimentation velocity and gel filtration assays	Homo sapiens

Synonyms

Synonyms	Comment	Organism
spastin AAA domain	-	Homo sapiens

General Information

General Information	Comment	Organism
malfunction	point mutations or exon deletions in the microtubule-severing ATPase, spastin, are responsible for approximately 40% of cases of autosomal dominant hereditary spastic paraplegia	Homo sapiens

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Release 2023.1 (January 2023)