Crystal structure of auxin-binding protein 1 in complex with auxin

EMBO J. 2002 Jun 17;21(12):2877-85. doi: 10.1093/emboj/cdf291.

Abstract

The structure of auxin-binding protein 1 (ABP1) from maize has been determined at 1.9 A resolution, revealing its auxin-binding site. The structure confirms that ABP1 belongs to the ancient and functionally diverse germin/seed storage 7S protein superfamily. The binding pocket of ABP1 is predominantly hydrophobic with a metal ion deep inside the pocket coordinated by three histidines and a glutamate. Auxin binds within this pocket, with its carboxylate binding the zinc and its aromatic ring binding hydrophobic residues including Trp151. There is a single disulfide between Cys2 and Cys155. No conformational rearrangement of ABP1 was observed when auxin bound to the protein in the crystal, but examination of the structure reveals a possible mechanism of signal transduction.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Crystallography, X-Ray
  • Indoleacetic Acids / chemistry*
  • Indoleacetic Acids / metabolism
  • Models, Molecular
  • Molecular Sequence Data
  • Molecular Structure
  • Plant Proteins / chemistry
  • Plant Proteins / genetics
  • Plant Proteins / metabolism
  • Protein Binding
  • Protein Structure, Tertiary*
  • Receptors, Cell Surface / chemistry*
  • Receptors, Cell Surface / genetics
  • Receptors, Cell Surface / metabolism
  • Sequence Alignment

Substances

  • Indoleacetic Acids
  • Plant Proteins
  • Receptors, Cell Surface
  • auxin-binding protein 1

Associated data

  • PDB/1LR5
  • PDB/1LRH