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1uhn

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(New page: 200px<br /><applet load="1uhn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uhn, resolution 2.1&Aring;" /> '''The crystal structure...)
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[[Image:1uhn.jpg|left|200px]]<br /><applet load="1uhn" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1uhn.jpg|left|200px]]<br /><applet load="1uhn" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1uhn, resolution 2.1&Aring;" />
caption="1uhn, resolution 2.1&Aring;" />
'''The crystal structure of the calcium binding protein AtCBL2 from Arabidopsis thaliana'''<br />
'''The crystal structure of the calcium binding protein AtCBL2 from Arabidopsis thaliana'''<br />
==Overview==
==Overview==
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Arabidopsis thaliana calcineurin B-like protein (AtCBL2) is a member of a, recently identified family of calcineurin B-like calcium-binding proteins, in A. thaliana. The crystal structure of AtCBL2 has been determined at 2.1, A resolution. The protein forms a compact alpha-helical structure with two, pairs of EF-hand motifs. The structure is similar in overall folding, topology to the structures of calcineurin B and neuronal calcium sensor 1, but differs significantly in local conformation. The two calcium ions are, coordinated in the first and fourth EF-hand motifs, whereas the second and, third EF-hand motifs are maintained in the open form by internal hydrogen, bonding without coordination of calcium ions. Both a possible site and a, possible mechanism for the target binding to AtCBL2 are discussed based on, the three-dimensional structure.
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Arabidopsis thaliana calcineurin B-like protein (AtCBL2) is a member of a recently identified family of calcineurin B-like calcium-binding proteins in A. thaliana. The crystal structure of AtCBL2 has been determined at 2.1 A resolution. The protein forms a compact alpha-helical structure with two pairs of EF-hand motifs. The structure is similar in overall folding topology to the structures of calcineurin B and neuronal calcium sensor 1, but differs significantly in local conformation. The two calcium ions are coordinated in the first and fourth EF-hand motifs, whereas the second and third EF-hand motifs are maintained in the open form by internal hydrogen bonding without coordination of calcium ions. Both a possible site and a possible mechanism for the target binding to AtCBL2 are discussed based on the three-dimensional structure.
==About this Structure==
==About this Structure==
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1UHN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UHN OCA].
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1UHN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UHN OCA].
==Reference==
==Reference==
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[[Category: calcium binding protein]]
[[Category: calcium binding protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 04:08:13 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:24:37 2008''

Revision as of 13:24, 21 February 2008


1uhn, resolution 2.1Å

Drag the structure with the mouse to rotate

The crystal structure of the calcium binding protein AtCBL2 from Arabidopsis thaliana

Overview

Arabidopsis thaliana calcineurin B-like protein (AtCBL2) is a member of a recently identified family of calcineurin B-like calcium-binding proteins in A. thaliana. The crystal structure of AtCBL2 has been determined at 2.1 A resolution. The protein forms a compact alpha-helical structure with two pairs of EF-hand motifs. The structure is similar in overall folding topology to the structures of calcineurin B and neuronal calcium sensor 1, but differs significantly in local conformation. The two calcium ions are coordinated in the first and fourth EF-hand motifs, whereas the second and third EF-hand motifs are maintained in the open form by internal hydrogen bonding without coordination of calcium ions. Both a possible site and a possible mechanism for the target binding to AtCBL2 are discussed based on the three-dimensional structure.

About this Structure

1UHN is a Single protein structure of sequence from Arabidopsis thaliana with as ligand. Full crystallographic information is available from OCA.

Reference

The crystal structure of the novel calcium-binding protein AtCBL2 from Arabidopsis thaliana., Nagae M, Nozawa A, Koizumi N, Sano H, Hashimoto H, Sato M, Shimizu T, J Biol Chem. 2003 Oct 24;278(43):42240-6. Epub 2003 Jul 19. PMID:12871972

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