PDBsum entry 1oof

Transport protein

PDB id: 1oof

Contents

Protein chains

124 a.a. *

Ligands

ACT ×4

EOH ×2

Waters ×234

* Residue conservation analysis

PDB id:

1oof

Name:

Transport protein

Title:

Complex of drosophila odorant binding protein lush with ethanol

Structure:

Odorant binding protein lush. Chain: a, b. Engineered: yes

Source:

Drosophila melanogaster. Fruit fly. Organism_taxid: 7227. Strain: oregon r. Tissue: subset of trichoid olfactory sensilla. Gene: lush. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

1.49Å R-factor: 0.181 R-free: 0.210

Authors:

S.W.Kruse,R.Zhao,D.P.Smith,D.N.M.Jones

Key ref:

S.W.Kruse et al. (2003). Structure of a specific alcohol-binding site defined by the odorant binding protein LUSH from Drosophila melanogaster. Nat Struct Biol, 10, 694-700. PubMed id: 12881720 DOI: 10.1038/nsb960

Date:

03-Mar-03 Release date: 02-Sep-03

Protein chains

O02372  (OB76A_DROME) -  General odorant-binding protein lush from Drosophila melanogaster

Seq: 153 a.a.

Struc: 124 a.a.

DOI no: 10.1038/nsb960

Nat Struct Biol 10:694-700 (2003)

PubMed id: 12881720

Structure of a specific alcohol-binding site defined by the odorant binding protein LUSH from Drosophila melanogaster.

S.W.Kruse, R.Zhao, D.P.Smith, D.N.Jones.

ABSTRACT

We have solved the high-resolution crystal structures of the Drosophila melanogaster alcohol-binding protein LUSH in complex with a series of short-chain n-alcohols. LUSH is the first known nonenzyme protein with a defined in vivo alcohol-binding function. The structure of LUSH reveals a set of molecular interactions that define a specific alcohol-binding site. A group of amino acids, Thr57, Ser52 and Thr48, form a network of concerted hydrogen bonds between the protein and the alcohol that provides a structural motif to increase alcohol-binding affinity at this site. This motif seems to be conserved in a number of mammalian ligand-gated ion channels that are directly implicated in the pharmacological effects of alcohol. Further, these sequences are found in regions of ion channels that are known to confer alcohol sensitivity. We suggest that the alcohol-binding site in LUSH represents a general model for alcohol-binding sites in proteins.

Selected figure(s)

Figure 1.
Figure 1. Ribbon diagrams of LUSH and PBP. (a) Diagram of LUSH -butanol structure solved to 1.25-Å resolution. Individual helices are labeled 1 - 6. 5' is a stretch of 3[10]-helix. Butanol is represented as a space-filling model at the center of the protein. Alkyl chain, cyan; hydroxyl group, red. (b) Diagram of PBP -bombykol complex from B. mori. Elements of secondary structure are colored as for LUSH. Bombykol is shown in a ball-and-stick representation.

Figure 2.
Figure 2. Structure of LUSH alcohol-binding pocket. (a) Key residues in alcohol-binding pocket formed by helix 3 (gold), helix 6 (blue) and the C-terminal strand. Network of hydrogen bonds formed by Thr48, Ser52, Thr57 and ethanol, red dotted lines. (b) Stereo view of electron density of residues in binding pocket of LUSH -ethanol complex. (c) Same view of alcohol-binding pocket in LUSH -butanol complex.

The above figures are reprinted by permission from Macmillan Publishers Ltd: Nat Struct Biol (2003, 10, 694-700) copyright 2003.

Figures were selected by an automated process.