PDBsum entry 1h8h

Hydrolase

PDB id: 1h8h

Contents

Protein chains

487 a.a. *

467 a.a. *

122 a.a. *

Ligands

ATP ×4

GOL

ADP

PO4

Metals

_MG ×5

Waters ×111

* Residue conservation analysis

References listed in PDB file

Key reference

• Title: The structure and nucleotide occupancy of bovine mitochondrial f(1)-Atpase are not influenced by crystallisation at high concentrations of nucleotide.
• Authors: R.I.Menz, A.G.Leslie, J.E.Walker.
• Ref.: FEBS Lett, 2001, 494, 11-14. [DOI no: 10.1016/S0014-5793(01)02302-X]
• PubMed id: 11297725

Abstract

Analysis of tryptophan mutants of F(1)-ATPase from Escherichia coli [Löbau et suggested that nucleotide concentrations used to grow crystals for the determination of the structure of bovine F(1)-ATPase would be sufficient to occupy only two catalytic sites, and that higher concentrations of nucleotide would result in all three sites being occupied. We have determined the structure of bovine F(1)-ATPase at 2.9 A resolution with crystals grown in the presence of 5 mM AMPPNP and 5 microM ADP. Similar to previous structures of bovine F(1)-ATPase determined with crystals grown in the presence of lower nucleotide concentrations, only two beta-subunits have bound nucleotide and the third subunit remains empty.

Figure 1.
Fig. 1. Stereo view of a superposition of the β[E] catalytic sites of the high AMPPNP and frozen-native [16] structures. All α-carbon atoms were used to superimpose the β[E]-subunits with rmsd of 0.15 Å. There is a slightly larger difference in the position of the bound phosphate (or sulphate) group, but this group has a very high temperature factor (80 Å^2). The carbon, nitrogen, oxygen and phosphorous atoms are coloured yellow, blue, red and pink, respectively. The 2F[o]–F[c] electron density map for the high AMPPNP structure is shown contoured at 1.3 σ.

The above figure is reprinted by permission from the Federation of European Biochemical Societies: FEBS Lett (2001, 494, 11-14) copyright 2001.

Secondary reference #1

• Title: Structure at 2.8 a resolution of f1-Atpase from bovine heart mitochondria.
• Authors: J.P.Abrahams, A.G.Leslie, R.Lutter, J.E.Walker.
• Ref.: Nature, 1994, 370, 621-628.
• PubMed id: 8065448

Secondary reference #2

• Title: Crystallization of f1-Atpase from bovine heart mitochondria.
• Authors: R.Lutter, J.P.Abrahams, M.J.Van raaij, R.J.Todd, T.Lundqvist, S.K.Buchanan, A.G.Leslie, J.E.Walker.
• Ref.: J Mol Biol, 1993, 229, 787-790.
• PubMed id: 8433373

Secondary reference #3

• Title: Inherent asymmetry of the structure of f1-Atpase from bovine heart mitochondria at 6.5 a resolution.
• Authors: J.P.Abrahams, R.Lutter, R.J.Todd, M.J.Van raaij, A.G.Leslie, J.E.Walker.
• Ref.: Embo J, 1993, 12, 1775-1780.
• PubMed id: 8491170