1lr5
From Proteopedia
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[[Image:1lr5.gif|left|200px]] | [[Image:1lr5.gif|left|200px]] | ||
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'''Crystal structure of auxin binding protein''' | '''Crystal structure of auxin binding protein''' | ||
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[[Category: Venis, M.]] | [[Category: Venis, M.]] | ||
[[Category: Woo, E J.]] | [[Category: Woo, E J.]] | ||
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| - | [[Category: | + | [[Category: Germin-like protein]] |
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Revision as of 21:12, 2 May 2008
Crystal structure of auxin binding protein
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
1LR5 is a Single protein structure of sequence from Zea mays. 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 Sat May 3 00:12:21 2008
