Structure of the C2A domain of rabphilin-3A

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.

Medienart:

Artikel

Erscheinungsjahr:

2006

Erschienen:

2006

Enthalten in:

Zur Gesamtaufnahme - volume:62

Enthalten in:

Acta crystallographica. Section D, Biological crystallography - 62(2006), Pt 7 vom: 22. Juli, Seite 793-9

Sprache:

Englisch

Beteiligte Personen:

Biadene, Marianna [VerfasserIn]
Montaville, Pierre [VerfasserIn]
Sheldrick, George M [VerfasserIn]
Becker, Stefan [VerfasserIn]

Themen:

Adaptor Proteins, Signal Transducing
Calcium
Calcium-Binding Proteins
Journal Article
Nerve Tissue Proteins
Peptide Fragments
Research Support, Non-U.S. Gov't
SY7Q814VUP
Vesicular Transport Proteins

Anmerkungen:

Date Completed 24.08.2006

Date Revised 13.12.2023

published: Print-Electronic

Citation Status MEDLINE

Förderinstitution / Projekttitel:

PPN (Katalog-ID):

NLM163661839