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 |
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Erscheinungsjahr: |
2006 |
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Erschienen: |
2006 |
Enthalten in: |
Zur Gesamtaufnahme - volume:62 |
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Enthalten in: |
Acta crystallographica. Section D, Biological crystallography - 62(2006), Pt 7 vom: 22. Juli, Seite 793-9 |
Sprache: |
Englisch |
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Beteiligte Personen: |
Biadene, Marianna [VerfasserIn] |
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Themen: |
Adaptor Proteins, Signal Transducing |
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Anmerkungen: |
Date Completed 24.08.2006 Date Revised 13.12.2023 published: Print-Electronic Citation Status MEDLINE |
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Förderinstitution / Projekttitel: |
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PPN (Katalog-ID): |
NLM163661839 |
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100 | 1 | |a Biadene, Marianna |e verfasserin |4 aut | |
245 | 1 | 0 | |a Structure of the C2A domain of rabphilin-3A |
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500 | |a Date Completed 24.08.2006 | ||
500 | |a Date Revised 13.12.2023 | ||
500 | |a published: Print-Electronic | ||
500 | |a Citation Status MEDLINE | ||
520 | |a 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 | ||
650 | 4 | |a Journal Article | |
650 | 4 | |a Research Support, Non-U.S. Gov't | |
650 | 7 | |a Adaptor Proteins, Signal Transducing |2 NLM | |
650 | 7 | |a Calcium-Binding Proteins |2 NLM | |
650 | 7 | |a Nerve Tissue Proteins |2 NLM | |
650 | 7 | |a Peptide Fragments |2 NLM | |
650 | 7 | |a Vesicular Transport Proteins |2 NLM | |
650 | 7 | |a Calcium |2 NLM | |
650 | 7 | |a SY7Q814VUP |2 NLM | |
700 | 1 | |a Montaville, Pierre |e verfasserin |4 aut | |
700 | 1 | |a Sheldrick, George M |e verfasserin |4 aut | |
700 | 1 | |a Becker, Stefan |e verfasserin |4 aut | |
773 | 0 | 8 | |i Enthalten in |t Acta crystallographica. Section D, Biological crystallography |d 1993 |g 62(2006), Pt 7 vom: 22. Juli, Seite 793-9 |w (DE-627)NLM092582249 |x 1399-0047 |7 nnns |
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