PDBsum entry 1nsf

Protein transport

PDB id: 1nsf

Contents

Protein chain

247 a.a. *

Ligands

ATP

Metals

_MG

Waters ×122

* Residue conservation analysis

PDB id:

1nsf

Name:

Protein transport

Title:

D2 hexamerization domain of n-ethylmaleimide sensitive factor (nsf)

Structure:

N-ethylmaleimide sensitive factor. Chain: a. Fragment: d2 hexamerization domain. Synonym: vesicular-fusion protein nsf. Engineered: yes

Source:

Cricetulus griseus. Chinese hamster. Organism_taxid: 10029. Cell_line: cho. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Biol. unit:

Hexamer (from PDB file)

Resolution:

1.90Å R-factor: 0.224 R-free: 0.244

Authors:

R.C.Yu,P.I.Hanson,R.Jahn,A.T.Brunger

Key ref:

R.C.Yu et al. (1998). Structure of the ATP-dependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATP. Nat Struct Biol, 5, 803-811. PubMed id: 9731775 DOI: 10.1038/1843

Date:

26-Jun-98 Release date: 25-Nov-98

Protein chain

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

Seq: 744 a.a.

Struc: 247 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 = ATP) corresponds exactly) + H2O = ADP + phosphate + H(+)

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

reference

DOI no: 10.1038/1843

Nat Struct Biol 5:803-811 (1998)

PubMed id: 9731775

Structure of the ATP-dependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATP.

R.C.Yu, P.I.Hanson, R.Jahn, A.T.Brünger.

ABSTRACT

N-ethylmaleimide-sensitive factor (NSF) is a hexameric ATPase which primes and/or dissociates SNARE complexes involved in intracellular fusion events. Each NSF protomer contains three domains: an N-terminal domain required for SNARE binding and two ATPase domains, termed D1 and D2, with D2 being required for oligomerization. We have determined the 1.9 A crystal structure of the D2 domain of NSF complexed with ATP using multi-wavelength anomalous dispersion phasing. D2 consists of a nucleotide binding subdomain with a Rossmann fold and a C-terminal subdomain, which is structurally unique among nucleotide binding proteins. There are interactions between the ATP moiety and both the neighboring D2 protomer and the C-terminal subdomain that may be important for ATP-dependent oligomerization. Of particular importance are three well-ordered and conserved lysine residues that form ionic interactions with the beta- and gamma-phosphates, one of which likely contributes to the low hydrolytic activity of D2.

Selected figure(s)

Figure 2.
Figure 2. Magnesium ion, in white, is coordinated by Thr 550, three water molecules (one of which is coordinated by Asp 603), and [222]beta - and [223]gamma -phosphate oxygens. Prepared using gl-render, Bobscript^[224]42, and rendered using POV-ray^[225]43. a, Stereoview of experimental electron density map using MAD phases. b, Stereoview of phase-combined 2F[o]-F[c] *sgr;[A]-weighted electron density maps using MAD and model phases of the refined model.

Figure 6.
Figure 6. a,Contact regions between subdomains of a protomer, in red and orange, and between neighboring protomers, in yellow and purple. b, The N-terminal and C-terminal subdomains contact through a hydrophobic patch consisting of Ile 508 and Trp 510 from the former (red), and Ile 670, Leu 682, and Leu 683 from the latter (orange). c, Between N-terminal subdomains on neighboring protomers, another hydrophobic contact is formed between Ile 574, Val 612, and Ile 614 from one protomer (purple) and the - through -carbons of Lys 586, Leu 609, Phe 618 and Val 628 from the other (yellow).

The above figures are reprinted by permission from Macmillan Publishers Ltd: Nat Struct Biol (1998, 5, 803-811) copyright 1998.

Figures were selected by an automated process.