PDBsum entry 2chd

Protein transport

PDB id: 2chd

Contents

Protein chain

129 a.a. *

Ligands

GOL

Waters ×66

* Residue conservation analysis

PDB id:

2chd

Name:

Protein transport

Title:

Crystal structure of the c2a domain of rabphilin-3a

Structure:

Rabphilin-3a. Chain: a. Fragment: c2a domain, residues 371-510. Synonym: exophilin-1. Engineered: yes

Source:

Rattus norvegicus. Rat. Organism_taxid: 10116. Expressed in: escherichia coli. Expression_system_taxid: 511693.

Resolution:

1.92Å R-factor: 0.201 R-free: 0.269

Authors:

M.Biadene,P.Montaville,G.M.Sheldrick,S.Becker

Key ref:

M.Biadene et al. (2006). Structure of the C2A domain of rabphilin-3A. Acta Crystallogr D Biol Crystallogr, 62, 793-799. PubMed id: 16790935 DOI: 10.1107/S0907444906017537

Date:

14-Mar-06 Release date: 28-Jun-06

Protein chain

P47709  (RP3A_RAT) -  Rabphilin-3A from Rattus norvegicus

Seq: 684 a.a.

Struc: 129 a.a.

DOI no: 10.1107/S0907444906017537

Acta Crystallogr D Biol Crystallogr 62:793-799 (2006)

PubMed id: 16790935

Structure of the C2A domain of rabphilin-3A.

M.Biadene, P.Montaville, G.M.Sheldrick, S.Becker.

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.

Selected figure(s)

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.

Figures were selected by an automated process.