PDBsum entry 1ngc

Hydrolase(acting on acid anhydrides)

PDB id: 1ngc

Contents

Protein chain

378 a.a. *

Ligands

PO4

ADP

Metals

_MG

Waters ×141

* Residue conservation analysis

PDB id:

1ngc

Name:

Hydrolase(acting on acid anhydrides)

Title:

Structural basis of the 70-kilodalton heat shock cognate protein atp hydrolytic activity, ii. Structure of the active site with adp or atp bound to wild type and mutant atpase fragment

Structure:

Heat-shock cognate 70 kd protein. Chain: a. Engineered: yes

Source:

Bos taurus. Cattle. Organism_taxid: 9913. Organ: brain

Resolution:

2.20Å R-factor: 0.188

Authors:

K.M.Flaherty,S.M.Wilbanks,C.Deluca-Flaherty,D.B.Mckay

Key ref:

K.M.Flaherty et al. (1994). Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. II. Structure of the active site with ADP or ATP bound to wild type and mutant ATPase fragment. J Biol Chem, 269, 12899-12907. PubMed id: 8175707

Date:

17-May-94 Release date: 31-Aug-94

Protein chain

P19120  (HSP7C_BOVIN) -  Heat shock cognate 71 kDa protein from Bos taurus

Seq: 650 a.a.

Struc: 378 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.3.6.4.10 - non-chaperonin molecular chaperone ATPase.
• Reaction: ATP + H2O = ADP + phosphate + H⁺

ATP + H2O = ADP (Bound ligand (Het Group name = ADP) corresponds exactly) + phosphate + H(+) (Bound ligand (Het Group name = PO4) corresponds exactly)

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

reference

J Biol Chem 269:12899-12907 (1994)

PubMed id: 8175707

Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. II. Structure of the active site with ADP or ATP bound to wild type and mutant ATPase fragment.

K.M.Flaherty, S.M.Wilbanks, C.DeLuca-Flaherty, D.B.McKay.

ABSTRACT

The ATPase fragment of the bovine 70-kDa heat shock cognate protein is an attractive construct in which to study its mechanism of ATP hydrolysis. The three-dimensional structure suggests several residues that might participate in the ATPase reaction. Four acidic residues (Asp-10, Glu-175, Asp-199, and Asp-206) have been individually mutated to both the cognate amine (asparagine/glutamine) and to serine, and the effects of the mutations on the kinetics of the ATPase activity (Wilbanks, S. M., DeLuca-Flaherty, C., and McKay, D. B. (1994) J. Biol. Chem. 269, 12893-12898) and the structure of the mutant ATPase fragments have been determined, typically to approximately 2.4 A resolution. Additionally, the structures of the wild type protein complexed with MgADP and Pi, MgAMPPNP (5'-adenylyl-beta, gamma-imidodiphosphate) and CaAMPPNP have been refined to 2.1, 2.4, and 2.4 A, respectively. Combined, these structures provide models for the prehydrolysis, MgATP-bound state and the post-hydrolysis, MgADP-bound state of the ATPase fragment. These models suggest a pathway for the hydrolytic reaction in which 1) the gamma phosphate of bound ATP reorients to form a beta, gamma-bidentate phosphate complex with the Mg2+ ion, allowing 2) in-line nucleophilic attack on the gamma phosphate by a H2O molecule or OH- ion, with 3) subsequent release of inorganic phosphate.