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2cjt
From Proteopedia
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|PDB= 2cjt |SIZE=350|CAPTION= <scene name='initialview01'>2cjt</scene>, resolution 1.44Å | |PDB= 2cjt |SIZE=350|CAPTION= <scene name='initialview01'>2cjt</scene>, resolution 1.44Å | ||
|SITE= <scene name='pdbsite=AC1:Fmt+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Fmt+Binding+Site+For+Chain+A'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene> | + | |LIGAND= <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cjt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cjt OCA], [http://www.ebi.ac.uk/pdbsum/2cjt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2cjt RCSB]</span> | ||
}} | }} | ||
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[[Category: Sudhof, T C.]] | [[Category: Sudhof, T C.]] | ||
[[Category: Tomchick, D R.]] | [[Category: Tomchick, D R.]] | ||
| - | [[Category: EDO]] | ||
| - | [[Category: FMT]] | ||
[[Category: alternative splicing]] | [[Category: alternative splicing]] | ||
[[Category: c2 domain]] | [[Category: c2 domain]] | ||
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[[Category: zinc finger]] | [[Category: zinc finger]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:22:30 2008'' |
Revision as of 23:22, 30 March 2008
| |||||||
| , resolution 1.44Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURAL BASIS FOR A MUNC13-1 HOMODIMER- MUNC13-1- RIM HETERODIMER SWITCH: C2-DOMAINS AS VERSATILE PROTEIN-PROTEIN INTERACTION MODULES
Overview
C(2) domains are well characterized as Ca(2+)/phospholipid-binding modules, but little is known about how they mediate protein-protein interactions. In neurons, a Munc13-1 C(2)A-domain/RIM zinc-finger domain (ZF) heterodimer couples synaptic vesicle priming to presynaptic plasticity. We now show that the Munc13-1 C(2)A domain homodimerizes, and that homodimerization competes with Munc13-1/RIM heterodimerization. X-ray diffraction studies guided by nuclear magnetic resonance (NMR) experiments reveal the crystal structures of the Munc13-1 C(2)A-domain homodimer and the Munc13-1 C(2)A-domain/RIM ZF heterodimer at 1.44 A and 1.78 A resolution, respectively. The C(2)A domain adopts a beta-sandwich structure with a four-stranded concave side that mediates homodimerization, leading to the formation of an eight-stranded beta-barrel. In contrast, heterodimerization involves the bottom tip of the C(2)A-domain beta-sandwich and a C-terminal alpha-helical extension, which wrap around the RIM ZF domain. Our results describe the structural basis for a Munc13-1 homodimer-Munc13-1/RIM heterodimer switch that may be crucial for vesicle priming and presynaptic plasticity, uncovering at the same time an unexpected versatility of C(2) domains as protein-protein interaction modules, and illustrating the power of combining NMR spectroscopy and X-ray crystallography to study protein complexes.
About this Structure
2CJT is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Structural basis for a Munc13-1 homodimer to Munc13-1/RIM heterodimer switch., Lu J, Machius M, Dulubova I, Dai H, Sudhof TC, Tomchick DR, Rizo J, PLoS Biol. 2006 Jul;4(7):e192. PMID:16732694
Page seeded by OCA on Mon Mar 31 02:22:30 2008
Categories: Rattus norvegicus | Single protein | Dai, H. | Dulubova, I. | Lu, J. | Machius, M. | Rizo, J. | Sudhof, T C. | Tomchick, D R. | Alternative splicing | C2 domain | Coiled coil | Exocytosis | Metal-binding | Munc13 | Neurotransmitter release | Phorbol-ester binding | Protein-protein interaction | Rim | Synaptosome | Zinc | Zinc finger
