PDBsum entry 3j94

Hydrolase

PDB id: 3j94

Contents

Protein chains

490 a.a.

466 a.a.

Ligands

ATP ×11

PDB id:

3j94

Name:

Hydrolase

Title:

Structure of atp-bound n-ethylmaleimide sensitive factor determined by single particle cryoelectron microscopy

Structure:

Vesicle-fusing atpase. Chain: a, b, c, d, e, f. Synonym: n-ethylmaleimide-sensitive fusion protein, nem-sensitive fusion protein, vesicular-fusion protein nsf, n-ethylmaleimide sensitive factor. Engineered: yes

Source:

Cricetulus griseus. Chinese hamster. Organism_taxid: 10029. Gene: nsf. Expressed in: escherichia coli. Expression_system_taxid: 562

Authors:

M.Zhao,S.Wu,Y.Cheng,A.T.Brunger

Key ref:

M.Zhao et al. (2015). Mechanistic insights into the recycling machine of the SNARE complex. Nature, 518, 61-67. PubMed id: 25581794 DOI: 10.1038/nature14148

Date:

05-Dec-14 Release date: 28-Jan-15

Protein chains

P18708  (NSF_CRIGR) -  Vesicle-fusing ATPase from Cricetulus griseus

Seq: 744 a.a.

Struc: 490 a.a.

Protein chain

P18708  (NSF_CRIGR) -  Vesicle-fusing ATPase from Cricetulus griseus

Seq: 744 a.a.

Struc: 466 a.a.

Enzyme reactions

• Enzyme class: Chains A, B, C, D, E, F: E.C.3.6.4.6 - vesicle-fusing ATPase.
• Reaction: ATP + H2O = ADP + phosphate + H⁺

ATP (Bound ligand (Het Group name = ATP) corresponds exactly) + H2O = ADP + phosphate + H(+)

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

reference

DOI no: 10.1038/nature14148

Nature 518:61-67 (2015)

PubMed id: 25581794

Mechanistic insights into the recycling machine of the SNARE complex.

M.Zhao, S.Wu, Q.Zhou, S.Vivona, D.J.Cipriano, Y.Cheng, A.T.Brunger.

ABSTRACT

Evolutionarily conserved SNARE (soluble N-ethylmaleimide sensitive factor attachment protein receptors) proteins form a complex that drives membrane fusion in eukaryotes. The ATPase NSF (N-ethylmaleimide sensitive factor), together with SNAPs (soluble NSF attachment protein), disassembles the SNARE complex into its protein components, making individual SNAREs available for subsequent rounds of fusion. Here we report structures of ATP- and ADP-bound NSF, and the NSF/SNAP/SNARE (20S) supercomplex determined by single-particle electron cryomicroscopy at near-atomic to sub-nanometre resolution without imposing symmetry. Large, potentially force-generating, conformational differences exist between ATP- and ADP-bound NSF. The 20S supercomplex exhibits broken symmetry, transitioning from six-fold symmetry of the NSF ATPase domains to pseudo four-fold symmetry of the SNARE complex. SNAPs interact with the SNARE complex with an opposite structural twist, suggesting an unwinding mechanism. The interfaces between NSF, SNAPs, and SNAREs exhibit characteristic electrostatic patterns, suggesting how one NSF/SNAP species can act on many different SNARE complexes.