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1lrh
From Proteopedia
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Crystal structure of auxin-binding protein 1 in complex with 1-naphthalene acetic acid
Overview
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.
About this Structure
1LRH is a Single protein structure of sequence from Zea mays with ZN and NLA as ligands. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Tue Nov 20 20:48:32 2007
