2cm5
From Proteopedia
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| - | [[Image:2cm5.jpg|left|200px]] | + | [[Image:2cm5.jpg|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF THE C2B DOMAIN OF RABPHILIN''' | + | {{Structure |
| + | |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> | ||
| + | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF THE C2B DOMAIN OF RABPHILIN''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2CM5 is a [ | + | 2CM5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CM5 OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17166855 17166855] |
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: zinc-finger]] | [[Category: zinc-finger]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:17:08 2008'' |
Revision as of 14:17, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE C2B DOMAIN OF RABPHILIN
Overview
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 Structure
2CM5 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 16:17:08 2008
