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Crystal structure of auxin‐binding protein 1 in complex with auxin
Author(s) -
Woo EuiJeon,
Marshall Jacqueline,
Bauly James,
Chen JinGui,
Venis Michael,
Napier Richard M.,
Pickersgill Richard W.
Publication year - 2002
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/cdf291
Subject(s) - queen (butterfly) , library science , art history , art , biology , botany , computer science , hymenoptera
The structure of auxin‐binding protein 1 (ABP1) from maize has been determined at 1.9 Å 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.