1b8c: Difference between revisions
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[[Image:1b8c.gif|left|200px]] | [[Image:1b8c.gif|left|200px]] | ||
'''PARVALBUMIN''' | {{Structure | ||
|PDB= 1b8c |SIZE=350|CAPTION= <scene name='initialview01'>1b8c</scene>, resolution 2.00Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''PARVALBUMIN''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1B8C is a [ | 1B8C is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Cyprinus_carpio Cyprinus carpio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B8C OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10545326 10545326] | ||
[[Category: Cyprinus carpio]] | [[Category: Cyprinus carpio]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: calcium binding protein]] | [[Category: calcium binding protein]] | ||
[[Category: calcium-binding]] | [[Category: calcium-binding]] | ||
[[Category: ef-hand | [[Category: ef-hand protein]] | ||
[[Category: parvalbumin]] | [[Category: parvalbumin]] | ||
''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 10:07:35 2008'' | ||
Revision as of 11:07, 20 March 2008
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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
1B8C 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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