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1ncx

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(New page: 200px<br /><applet load="1ncx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ncx, resolution 1.8&Aring;" /> '''TROPONIN C'''<br /> ...)
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[[Image:1ncx.jpg|left|200px]]<br /><applet load="1ncx" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ncx.jpg|left|200px]]<br /><applet load="1ncx" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ncx, resolution 1.8&Aring;" />
caption="1ncx, resolution 1.8&Aring;" />
'''TROPONIN C'''<br />
'''TROPONIN C'''<br />
==Overview==
==Overview==
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The crystal structures of three metal complexes of troponin C (TnC) have, been determined and refined where the two occupied structural Ca(2+) sites, in the C domain have been substituted by Mn(2+), Cd(2+) and Tb(3+). The, X-ray intensity data were collected to 2.1, 1.8 and 1.8 A resolution, respectively, on the three metal complexes, which are isomorphous with, Ca-TnC. The three complexes have r.m.s. deviations of 0.27, 0.25 and 0.35, A, respectively, for all protein atoms, from Ca-TnC. Irrespective of the, charge on the metal (+2 or +3), the occupied sites 3 and 4 exhibit a, distorted pentagonal bipyramidal coordination, like Ca-TnC, with seven, ligands, six from the 12-residue binding loop and the seventh from a water, molecule. Mn(2+) at site 4 seems to display a longer distance to one of, the carboxyl bidentate ligands representing an intermediate coordination, simulating the six-coordinate Mg(2+). The carboxyl O atoms of the, bidentate Glu12 are displaced on the side of the equatorial plane passing, through the remaining three ligands with one O atom closer to the plane, (Delta of 0.11 to 0.76 A) than the other (Delta of 0.93 to 1.38 A). The, two axial ligands are an aspartic carboxyl O atom and a water molecule., The metal is displaced (0.18 to 0.56 A) towards the water facing the water, channel.
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The crystal structures of three metal complexes of troponin C (TnC) have been determined and refined where the two occupied structural Ca(2+) sites in the C domain have been substituted by Mn(2+), Cd(2+) and Tb(3+). The X-ray intensity data were collected to 2.1, 1.8 and 1.8 A resolution, respectively, on the three metal complexes, which are isomorphous with Ca-TnC. The three complexes have r.m.s. deviations of 0.27, 0.25 and 0.35 A, respectively, for all protein atoms, from Ca-TnC. Irrespective of the charge on the metal (+2 or +3), the occupied sites 3 and 4 exhibit a distorted pentagonal bipyramidal coordination, like Ca-TnC, with seven ligands, six from the 12-residue binding loop and the seventh from a water molecule. Mn(2+) at site 4 seems to display a longer distance to one of the carboxyl bidentate ligands representing an intermediate coordination simulating the six-coordinate Mg(2+). The carboxyl O atoms of the bidentate Glu12 are displaced on the side of the equatorial plane passing through the remaining three ligands with one O atom closer to the plane (Delta of 0.11 to 0.76 A) than the other (Delta of 0.93 to 1.38 A). The two axial ligands are an aspartic carboxyl O atom and a water molecule. The metal is displaced (0.18 to 0.56 A) towards the water facing the water channel.
==About this Structure==
==About this Structure==
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1NCX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with CD and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NCX OCA].
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1NCX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with <scene name='pdbligand=CD:'>CD</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NCX OCA].
==Reference==
==Reference==
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[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Rao, S.T.]]
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[[Category: Rao, S T.]]
[[Category: Sundaralingam, M.]]
[[Category: Sundaralingam, M.]]
[[Category: CD]]
[[Category: CD]]
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[[Category: muscle protein]]
[[Category: muscle protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:08:52 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:04:44 2008''

Revision as of 12:04, 21 February 2008


1ncx, resolution 1.8Å

Drag the structure with the mouse to rotate

TROPONIN C

Overview

The crystal structures of three metal complexes of troponin C (TnC) have been determined and refined where the two occupied structural Ca(2+) sites in the C domain have been substituted by Mn(2+), Cd(2+) and Tb(3+). The X-ray intensity data were collected to 2.1, 1.8 and 1.8 A resolution, respectively, on the three metal complexes, which are isomorphous with Ca-TnC. The three complexes have r.m.s. deviations of 0.27, 0.25 and 0.35 A, respectively, for all protein atoms, from Ca-TnC. Irrespective of the charge on the metal (+2 or +3), the occupied sites 3 and 4 exhibit a distorted pentagonal bipyramidal coordination, like Ca-TnC, with seven ligands, six from the 12-residue binding loop and the seventh from a water molecule. Mn(2+) at site 4 seems to display a longer distance to one of the carboxyl bidentate ligands representing an intermediate coordination simulating the six-coordinate Mg(2+). The carboxyl O atoms of the bidentate Glu12 are displaced on the side of the equatorial plane passing through the remaining three ligands with one O atom closer to the plane (Delta of 0.11 to 0.76 A) than the other (Delta of 0.93 to 1.38 A). The two axial ligands are an aspartic carboxyl O atom and a water molecule. The metal is displaced (0.18 to 0.56 A) towards the water facing the water channel.

About this Structure

1NCX is a Single protein structure of sequence from Gallus gallus with and as ligands. Full crystallographic information is available from OCA.

Reference

X-ray structures of Mn, Cd and Tb metal complexes of troponin C., Rao ST, Satyshur KA, Greaser ML, Sundaralingam M, Acta Crystallogr D Biol Crystallogr. 1996 Sep 1;52(Pt 5):916-22. PMID:15299599

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