Publication Abstract from PubMed
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.
Crystal structure of auxin-binding protein 1 in complex with auxin.,Woo EJ, Marshall J, Bauly J, Chen JG, Venis M, Napier RM, Pickersgill RW EMBO J. 2002 Jun 17;21(12):2877-85. PMID:12065401[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
