1fw4

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(New page: 200px<br /><applet load="1fw4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fw4, resolution 1.7&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1fw4.gif|left|200px]]<br /><applet load="1fw4" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1fw4.gif|left|200px]]<br /><applet load="1fw4" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1fw4, resolution 1.7&Aring;" />
caption="1fw4, resolution 1.7&Aring;" />
'''CRYSTAL STRUCTURE OF E. COLI FRAGMENT TR2C FROM CALMODULIN TO 1.7 A RESOLUTION'''<br />
'''CRYSTAL STRUCTURE OF E. COLI FRAGMENT TR2C FROM CALMODULIN TO 1.7 A RESOLUTION'''<br />
==Overview==
==Overview==
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Fragment TR2C is the C-terminal part of the calcium-binding protein, calmodulin, including residues 78-148. The crystal structure of TR2C was, solved by molecular replacement and refined to a conventional R value of, 21.8% (R(free) = 22.0%), using all data in the resolution range 20.0-1.7, A. This study shows that the secondary structure of TR2C, a pair of, EF-hand motifs with two calcium-binding sites, is similar to the, corresponding motifs in intact calmodulin. However, it also indicates that, the N-terminus of helix E is closer to the C-terminus of helix H in TR2C, than in the intact protein and that the loop connecting the EF-hands shows, different conformations in the two structures. The crystal structure of, TR2C was further found to be similar to the set of NMR structures of this, fragment, although some pronounced differences exist.
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Fragment TR2C is the C-terminal part of the calcium-binding protein calmodulin, including residues 78-148. The crystal structure of TR2C was solved by molecular replacement and refined to a conventional R value of 21.8% (R(free) = 22.0%), using all data in the resolution range 20.0-1.7 A. This study shows that the secondary structure of TR2C, a pair of EF-hand motifs with two calcium-binding sites, is similar to the corresponding motifs in intact calmodulin. However, it also indicates that the N-terminus of helix E is closer to the C-terminus of helix H in TR2C than in the intact protein and that the loop connecting the EF-hands shows different conformations in the two structures. The crystal structure of TR2C was further found to be similar to the set of NMR structures of this fragment, although some pronounced differences exist.
==About this Structure==
==About this Structure==
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1FW4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. This structure superseeds the now removed PDB entry 1TRC. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FW4 OCA].
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1FW4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. This structure supersedes the now removed PDB entry 1TRC. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FW4 OCA].
==Reference==
==Reference==
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Olsson, L.L.]]
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[[Category: Olsson, L L.]]
[[Category: Sjolin, L.]]
[[Category: Sjolin, L.]]
[[Category: CA]]
[[Category: CA]]
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[[Category: tr2c]]
[[Category: tr2c]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:21:36 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:43:19 2008''

Revision as of 10:43, 21 February 2008

Image:1fw4.gif

1fw4, resolution 1.7Å

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CRYSTAL STRUCTURE OF E. COLI FRAGMENT TR2C FROM CALMODULIN TO 1.7 A RESOLUTION

Overview

Fragment TR2C is the C-terminal part of the calcium-binding protein calmodulin, including residues 78-148. The crystal structure of TR2C was solved by molecular replacement and refined to a conventional R value of 21.8% (R(free) = 22.0%), using all data in the resolution range 20.0-1.7 A. This study shows that the secondary structure of TR2C, a pair of EF-hand motifs with two calcium-binding sites, is similar to the corresponding motifs in intact calmodulin. However, it also indicates that the N-terminus of helix E is closer to the C-terminus of helix H in TR2C than in the intact protein and that the loop connecting the EF-hands shows different conformations in the two structures. The crystal structure of TR2C was further found to be similar to the set of NMR structures of this fragment, although some pronounced differences exist.

About this Structure

1FW4 is a Single protein structure of sequence from Bos taurus with as ligand. This structure supersedes the now removed PDB entry 1TRC. Full crystallographic information is available from OCA.

Reference

Structure of Escherichia coli fragment TR2C from calmodulin to 1.7 A resolution., Olsson LL, Sjolin L, Acta Crystallogr D Biol Crystallogr. 2001 May;57(Pt 5):664-9. Epub 2001, Apr 24. PMID:11320306

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