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5.6.1.1: microtubule-severing ATPase

This is an abbreviated version!
For detailed information about microtubule-severing ATPase, go to the full flat file.

Word Map on EC 5.6.1.1

Reaction

n ATP + n H2O +

a microtubule
= n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers

Synonyms

adseverin, Arabidopsis thaliana katanin small subunit, AtKSS, D-spastin, DGL1, Dm-Kat60, Drosophila katanin Dm-Kat60, EC 3.6.4.3, kananin, Kat60, katanin, KATANIN 1, katanin p60, katanin p60 ATPase-containing subunit A1, katanin p60 microtubule-severing protein, KATNAL1, kinesin spindle protein, kp60-NTD, KSP, mei-1, MEI-1/MEI-2 complex, MEI-1/MEI-2 katanin complex, microtuble severing AAA ATPase spastin, microtuble-severing AAA ATPase, microtuble-severing ATPase spastin, microtubule severing protein, microtubule-severing AAA ATPase, microtubule-severing ATPase, microtubule-severing complex katanin, microtubule-severing complex MEI-1/MEI-2 katanin, microtubule-severing protein, microtubule-stimulated ATPase, MT-severing AAA ATPase, P60, p60 KAT1p, p60 katanin, P60-kananin, P60-katanin, p81-p60, Pf15, plant microtubule-severing protein, rice KTN1, scinderin, SPAS-1, spastin, spastin AAA domain, SPG4, Sug1p, vertebrate katanin

ECTree

     5 Isomerases
         5.6 Isomerases altering macromolecular conformation
             5.6.1 Enzymes altering polypeptide conformation or assembly
                5.6.1.1 microtubule-severing ATPase

Crystallization

Crystallization on EC 5.6.1.1 - microtubule-severing ATPase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop method at 20°C, crystal structure of MEI-1 AAA ATPase in the ADP-bound state reveals a pseudo-hexameric left-handed spiral assembly
secondary structure analyzed by circular dichroism (CD) spectrum. SPAS-1 retains a high degree of alpha-helical structure
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the X-ray structure of the nucleotide-free, monomeric AAA domain of Drosophila melanogaster spastin, residues 464-758, is solved at a resolution of 2.7 A
crystals of spastin are grown using the vapor diffusion method at 20°C
hanging drop method, the N-terminal residues (about 10000 Da) are clipped off during time of crystal formation (5-7 days)
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hanging-drop method at 20°C, crystal structure of KATNAL1 AAA ATPase in the nucleotide-free state reveals a monomer
high-resolution structure of the heterodimeric complex of p60-microtubule interacting and trafficking domain and the p80 C-terminal domain is determined by X-ray crystallography
Q9WV86; Q8BG40
the structure of kp60-NTD reveals a striking similarity to those of the microtubule interacting and trafficking domains (MIT). The arragnement of helices 2 and 3 is well conserved between kp60-NTD and the MIT domain from Vps4, a homologous protein that promotes disassembly of the endosomal sorting complexes required for transport III membrane skeleton complex. The positively charged surface formed by helices 2 and 3 binds tubulin
-