PDBsum entry 5c18

Hydrolase

PDB id: 5c18

Contents

Protein chains

(+ 0 more) 722 a.a.

Ligands

AGS ×12

Metals

_CL ×6

_MG ×12

Waters ×30

PDB id:

5c18

Name:

Hydrolase

Title:

P97-delta709-728 in complex with atp-gamma-s

Structure:

Transitional endoplasmic reticulum atpase. Chain: a, b, c, d, e, f. Synonym: ter atpase,15s mg(2+)-atpase p97 subunit,valosin-containing protein,vcp. Engineered: yes. Mutation: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: vcp. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.

Resolution:

3.30Å R-factor: 0.213 R-free: 0.249

Authors:

P.Haenzelmann,H.Schindelin

Key ref:

P.Hänzelmann and H.Schindelin (2016). Structural Basis of ATP Hydrolysis and Intersubunit Signaling in the AAA+ ATPase p97. Structure, 24, 127-139. PubMed id: 26712278 DOI: 10.1016/j.str.2015.10.026

Date:

13-Jun-15 Release date: 13-Jan-16

Protein chains

P55072  (TERA_HUMAN) -  Transitional endoplasmic reticulum ATPase from Homo sapiens

Seq: 806 a.a.

Struc: 722 a.a.

Enzyme reactions

• Enzyme class: E.C.3.6.4.6 - vesicle-fusing ATPase.
• Reaction: ATP + H2O = ADP + phosphate + H⁺

ATP (Bound ligand (Het Group name = AGS) matches with 93.75% similarity) + H2O = ADP + phosphate + H(+)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1016/j.str.2015.10.026

Structure 24:127-139 (2016)

PubMed id: 26712278

Structural Basis of ATP Hydrolysis and Intersubunit Signaling in the AAA+ ATPase p97.

P.Hänzelmann, H.Schindelin.

ABSTRACT

p97 belongs to the superfamily of AAA+ ATPases and is characterized by a tandem AAA module, an N-terminal domain involved in substrate and cofactor interactions, and a functionally important unstructured C-terminal tail. The ATPase activity is controlled by an intradomain communication within the same protomer and an interdomain communication between neighboring protomers. Here, we present for the first time crystal structures in which the physiologically relevant p97 hexamer constitutes the content of the asymmetric unit, namely in the apo state without nucleotide in either the D1 or D2 module and in the pre-activated state with ATPγS bound to both modules. The structures provide new mechanistic insights into the interdomain communication mediated by conformational changes of the C terminus as well as an intersubunit signaling network, which couples the nucleotide state to the conformation of the central putative substrate binding pore.