1b8r: Difference between revisions
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|PDB= 1b8r |SIZE=350|CAPTION= <scene name='initialview01'>1b8r</scene>, resolution 1.9Å | |PDB= 1b8r |SIZE=350|CAPTION= <scene name='initialview01'>1b8r</scene>, resolution 1.9Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b8r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b8r OCA], [http://www.ebi.ac.uk/pdbsum/1b8r PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1b8r RCSB]</span> | |||
}} | }} | ||
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[[Category: Li, Q.]] | [[Category: Li, Q.]] | ||
[[Category: Potter, J D.]] | [[Category: Potter, J D.]] | ||
[[Category: calcium binding protein]] | [[Category: calcium binding protein]] | ||
[[Category: calcium-binding]] | [[Category: calcium-binding]] | ||
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[[Category: parvalbumin]] | [[Category: parvalbumin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:55:56 2008'' | ||
Revision as of 18:55, 30 March 2008
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| , resolution 1.9Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
PARVALBUMIN
OverviewOverview
BACKGROUND: The EF-hand family is a large set of Ca(2+)-binding proteins that contain characteristic helix-loop-helix binding motifs that are highly conserved in sequence. Members of this family include parvalbumin and many prominent regulatory proteins such as calmodulin and troponin C. EF-hand proteins are involved in a variety of physiological processes including cell-cycle regulation, second messenger production, muscle contraction, microtubule organization and vision. RESULTS: We have determined the structures of parvalbumin mutants designed to explore the role of the last coordinating residue of the Ca(2+)-binding loop. An E101D substitution has been made in the parvalbumin EF site. The substitution decreases the Ca(2+)-binding affinity 100-fold and increases the Mg(2+)-binding affinity 10-fold. Both the Ca(2+)- and Mg(2+)-bound structures have been determined, and a structural basis has been proposed for the metal-ion-binding properties. CONCLUSIONS: The E101D mutation does not affect the Mg(2+) coordination geometry of the binding loop, but it does pull the F helix 1.1 A towards the loop. The E101D-Ca(2+) structure reveals that this mutant cannot obtain the sevenfold coordination preferred by Ca(2+), presumably because of strain limits imposed by tertiary structure. Analysis of these results relative to previously reported structural information supports a model wherein the characteristics of the last coordinating residue and the plasticity of the Ca(2+)-binding loop delimit the allowable geometries for the coordinating sphere.
About this StructureAbout this Structure
1B8R is a Single protein structure of sequence from Cyprinus carpio. Full crystallographic information is available from OCA.
ReferenceReference
Metal-ion affinity and specificity in EF-hand proteins: coordination geometry and domain plasticity in parvalbumin., Cates MS, Berry MB, Ho EL, Li Q, Potter JD, Phillips GN Jr, Structure. 1999 Oct 15;7(10):1269-78. PMID:10545326
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