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PDBsum entry 2chd

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Protein transport PDB id
2chd
Contents
Protein chain
129 a.a.
Ligands
GOL
Waters ×66

References listed in PDB file
Key reference
Title Structure of the c2a domain of rabphilin-3a.
Authors M.Biadene, P.Montaville, G.M.Sheldrick, S.Becker.
Ref. Acta Crystallogr D Biol Crystallogr, 2006, 62, 793-799. [DOI no: 10.1107/S0907444906017537]
PubMed id 16790935
Abstract
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 consists of a large positively charged belt surrounded by two negatively charged patches located at both tips of the domain. In comparison, the structurally very similar C2A domain of synaptotagmin I has a highly acidic electrostatic surface, suggesting completely unrelated functions for these two C2A domains.
Figure 2.
Figure 2 Overall structure of the C2A domain of rabphilin-3A. (a) Cartoon drawing showing the common eight-stranded antiparallel -sandwich. (b) Topology diagram (made with the program TOPDRAW; Bond, 2003[Bond, C. S. (2003). Bioinformatics, 19, 311-312.]).
Figure 3.
Figure 3 Residues in the Ca^2+-binding region: the residues of the C2A domain of rabphilin-3A are coloured green and the residues of synaptotagmin I and the Ca^2+ ions present in that structure (PDB code 1byn ) are coloured blue.
The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2006, 62, 793-799) copyright 2006.
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