2CHD

Crystal structure of the C2A domain of Rabphilin-3A

Summary for 2CHD

• Entry DOI: 10.2210/pdb2chd/pdb
• Related: 1ZBD 3RPB
• Descriptor: RABPHILIN-3A, GLYCEROL (3 entities in total)
• Functional Keywords: rabphilin-3a, c2 domain, c2a, calcium binding, synaptic exocytosis, metal-binding, protein transport, synapse, transport, zinc-finger
• Biological source: RATTUS NORVEGICUS (RAT)
• Cellular location: Cell junction, synapse : P47709
• Total number of polymer chains: 1
• Total formula weight: 16308.41

Authors

Biadene, M.,Montaville, P.,Sheldrick, G.M.,Becker, S. (deposition date: 2006-03-14, release date: 2006-06-28, Last modification date: 2023-12-13)

Primary citation

Biadene, M.,Montaville, P.,Sheldrick, G.M.,Becker, S.
Structure of the C2A Domain of Rabphilin-3A.
Acta Crystallogr.,Sect.D, 62:793-, 2006

PubMed 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.

PubMed: 16790935
DOI: 10.1107/S0907444906017537

Experimental method

X-RAY DIFFRACTION (1.92 Å)