1OOH

Complex of Drosophila odorant binding protein LUSH with butanol

Summary for 1OOH

• Entry DOI: 10.2210/pdb1ooh/pdb
• Related: 1OOF 1OOG 1OOI
• Descriptor: odorant binding protein LUSH, ACETATE ION, 1-BUTANOL, ... (4 entities in total)
• Functional Keywords: lush, alcohol, odorant binding, transport protein
• Biological source: Drosophila melanogaster (fruit fly)
• Cellular location: Secreted: O02372
• Total number of polymer chains: 2
• Total formula weight: 29265.88

Authors

Kruse, S.W.,Zhao, R.,Smith, D.P.,Jones, D.N.M. (deposition date: 2003-03-03, release date: 2003-09-02, Last modification date: 2024-11-20)

Primary citation

Kruse, S.W.,Zhao, R.,Smith, D.P.,Jones, D.N.M.
Structure of a specific alcohol-binding site defined by the odorant binding protein LUSH from Drosophila melanogaster
Nat.Struct.Biol., 10:694-700, 2003

PubMed 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.

PubMed: 12881720
DOI: 10.1038/nsb960

Experimental method

X-RAY DIFFRACTION (1.25 Å)