5Z6Q

Crystal structure of AAA of Spastin

Summary for 5Z6Q

• Entry DOI: 10.2210/pdb5z6q/pdb
• Descriptor: Spastin, CHLORIDE ION (2 entities in total)
• Functional Keywords: spastin, hydrolase
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 1
• Total formula weight: 42780.28

Authors

Lin, Z.,Wang, C.,Shen, Y. (deposition date: 2018-01-25, release date: 2018-12-05, Last modification date: 2024-03-27)

Primary citation

Fan, X.,Lin, Z.,Fan, G.,Lu, J.,Hou, Y.,Habai, G.,Sun, L.,Yu, P.,Shen, Y.,Wen, M.,Wang, C.
The AAA protein spastin possesses two levels of basal ATPase activity
FEBS Lett., 592:1625-1633, 2018

PubMed Abstract: The AAA ATPase spastin is a microtubule-severing enzyme that plays important roles in various cellular events including axon regeneration. Herein, we found that the basal ATPase activity of spastin is negatively regulated by spastin concentration. By determining a spastin crystal structure, we demonstrate the necessity of intersubunit interactions between spastin AAA domains. Neutralization of the positive charges in the microtubule-binding domain (MTBD) of spastin dramatically decreases the ATPase activity at low concentration, although the ATP-hydrolyzing potential is not affected. These results demonstrate that, in addition to the AAA domain, the MTBD region of spastin is also involved in regulating ATPase activity, making interactions between spastin protomers more complicated than expected.

PubMed: 29710391
DOI: 10.1002/1873-3468.13075

Experimental method

X-RAY DIFFRACTION (3 Å)