2chd

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2chd, resolution 1.92Å

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CRYSTAL STRUCTURE OF THE C2A DOMAIN OF RABPHILIN-3A

Overview

Rabphilin-3A is a neuronal protein containing a C2-domain tandem. To date, only the structure of the C2B domain has been solved. The crystal, structure of the Ca2+-free C2A domain has been solved by molecular, replacement and refined to 1.92 A resolution. It adopts the classical, C2-domain fold consisting of an eight-stranded antiparallel beta-sandwich, with type I topology. In agreement with its Ca2+-dependent negatively, charged membrane-binding properties, this C2 domain contains all the, conserved acidic residues responsible for calcium binding. However, the, replacement of a conserved aspartic acid residue by glutamic acid allows, formation of an additional strong hydrogen bond, resulting in increased, rigidity of calcium-binding loop 1. The electrostatic surface of the C2A, domain ... [(full description)]

About this Structure

2CHD is a [Single protein] structure of sequence from [Rattus norvegicus] with GOL as [ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Structure of the C2A domain of rabphilin-3A., Biadene M, Montaville P, Sheldrick GM, Becker S, Acta Crystallogr D Biol Crystallogr. 2006 Jul;62(Pt 7):793-9. Epub 2006, Jun 20. PMID:16790935

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