2cm5: Difference between revisions
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|PDB= 2cm5 |SIZE=350|CAPTION= <scene name='initialview01'>2cm5</scene>, resolution 1.28Å | |PDB= 2cm5 |SIZE=350|CAPTION= <scene name='initialview01'>2cm5</scene>, resolution 1.28Å | ||
|SITE= <scene name='pdbsite=AC1:Ca+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Ca+Binding+Site+For+Chain+A'>AC1</scene> | ||
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cm5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cm5 OCA], [http://www.ebi.ac.uk/pdbsum/2cm5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2cm5 RCSB]</span> | |||
}} | }} | ||
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[[Category: Schlicker, C.]] | [[Category: Schlicker, C.]] | ||
[[Category: Sheldrick, G M.]] | [[Category: Sheldrick, G M.]] | ||
[[Category: c2 domain]] | [[Category: c2 domain]] | ||
[[Category: c2a-c2b linker fragment]] | [[Category: c2a-c2b linker fragment]] | ||
| Line 40: | Line 42: | ||
[[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 02:23:28 2008'' | ||
Revision as of 02:23, 31 March 2008
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| , resolution 1.28Å | |||||||
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| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE C2B DOMAIN OF RABPHILIN
OverviewOverview
The Ca(2+) binding properties of C2 domains are essential for the function of their host proteins. We present here the first crystal structures showing an unexpected Ca(2+) binding mode of the C2B domain of rabphilin-3A in atomic detail. Acidic residues from the linker region between the C2A and C2B domains of rabphilin-3A interact with the Ca(2+)-binding region of the C2B domain. Because of these interactions, the coordination sphere of the two bound Ca(2+) ions is almost complete. Mutation of these acidic residues to alanine resulted in a 10-fold decrease in the intrinsic Ca(2+) binding affinity of the C2B domain. Using NMR spectroscopy, we show that this interaction occurred only in the Ca(2+)-bound state of the C2B domain. In addition, this Ca(2+) binding mode was maintained in the C2 domain tandem fragment. In NMR-based liposome binding assays, the linker was not released upon phospholipid binding. Therefore, this unprecedented Ca(2+) binding mode not only shows how a C2 domain increases its intrinsic Ca(2+) affinity, but also provides the structural base for an atypical protein-Ca(2+)-phospholipid binding mode of rabphilin-3A.
About this StructureAbout this Structure
2CM5 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
ReferenceReference
The C2A-C2B linker defines the high affinity Ca(2+) binding mode of rabphilin-3A., Montaville P, Schlicker C, Leonov A, Zweckstetter M, Sheldrick GM, Becker S, J Biol Chem. 2007 Feb 16;282(7):5015-25. Epub 2006 Dec 13. PMID:17166855
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