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1j7r

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{{STRUCTURE_1j7r| PDB=1j7r | SCENE= }}
{{STRUCTURE_1j7r| PDB=1j7r | SCENE= }}
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'''Solution structure and backbone dynamics of the defunct EF-hand domain of Calcium Vector Protein'''
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===Solution structure and backbone dynamics of the defunct EF-hand domain of Calcium Vector Protein===
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==Overview==
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CaVP (calcium vector protein) is a Ca(2+) sensor of the EF-hand protein family which is highly abundant in the muscle of Amphioxus. Its three-dimensional structure is not known, but according to the sequence analysis, the protein is composed of two domains, each containing a pair of EF-hand motifs. We determined recently the solution structure of the C-terminal domain (Trp81-Ser161) and characterized the large conformational and dynamic changes induced by Ca(2+) binding. In contrast, the N-terminal domain (Ala1-Asp86) has lost the capacity to bind the metal ion due to critical mutations and insertions in the two calcium loops. In this paper, we report the solution structure of the N-terminal domain and its backbone dynamics based on NMR spectroscopy, nuclear relaxation, and molecular modeling. The well-resolved three-dimensional structure is typical of a pair of EF-hand motifs, joined together by a short antiparallel beta-sheet. The tertiary arrangement of the two EF-hands results in a closed-type conformation, with near-antiparallel alpha-helices, similar to other EF-hand pairs in the absence of calcium ions. To characterize the internal dynamics of the protein, we measured the (15)N nuclear relaxation rates and the heteronuclear NOE effect in (15)N-labeled N-CaVP at a magnetic field of 11.74 T and 298 K. The domain is mainly monomeric in solution and undergoes an isotropic Brownian rotational diffusion with a correlation time of 7.1 ns, in good agreement with the fluorescence anisotropy decay measurements. Data analysis using a model-free procedure showed that the amide backbone groups in the alpha-helices and beta-strands undergo highly restricted movements on a picosecond to nanosecond time scale. The amide groups in Ca(2+) binding loops and in the linker fragment also display rapid fluctuations with slightly increased amplitudes.
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(as it appears on PubMed at http://www.pubmed.gov), where 11705378 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11705378}}
==About this Structure==
==About this Structure==
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1J7R is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Branchiostoma_lanceolatum Branchiostoma lanceolatum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J7R OCA].
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1J7R is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Branchiostoma_lanceolatum Branchiostoma lanceolatum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J7R OCA].
==Reference==
==Reference==
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[[Category: Ef-hand]]
[[Category: Ef-hand]]
[[Category: Nmr]]
[[Category: Nmr]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:53:27 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 14:36:12 2008''

Revision as of 11:36, 1 July 2008

Image:1j7r.png

Template:STRUCTURE 1j7r

Solution structure and backbone dynamics of the defunct EF-hand domain of Calcium Vector Protein

Template:ABSTRACT PUBMED 11705378

About this Structure

1J7R is a Single protein structure of sequence from Branchiostoma lanceolatum. Full experimental information is available from OCA.

Reference

Solution structure and backbone dynamics of the defunct domain of calcium vector protein., Theret I, Baladi S, Cox JA, Gallay J, Sakamoto H, Craescu CT, Biochemistry. 2001 Nov 20;40(46):13888-97. PMID:11705378

Page seeded by OCA on Tue Jul 1 14:36:12 2008

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