4cln

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[[Image:4cln.gif|left|200px]]
[[Image:4cln.gif|left|200px]]
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{{Structure
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{{STRUCTURE_4cln| PDB=4cln | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4cln FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cln OCA], [http://www.ebi.ac.uk/pdbsum/4cln PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=4cln RCSB]</span>
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'''STRUCTURE OF A RECOMBINANT CALMODULIN FROM DROSOPHILA MELANOGASTER REFINED AT 2.2-ANGSTROMS RESOLUTION'''
'''STRUCTURE OF A RECOMBINANT CALMODULIN FROM DROSOPHILA MELANOGASTER REFINED AT 2.2-ANGSTROMS RESOLUTION'''
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[[Category: Sack, J S.]]
[[Category: Sack, J S.]]
[[Category: Taylor, D A.]]
[[Category: Taylor, D A.]]
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[[Category: calcium binding protein]]
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[[Category: Calcium binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:22:15 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:38:16 2008''
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Revision as of 19:22, 4 May 2008

Template:STRUCTURE 4cln

STRUCTURE OF A RECOMBINANT CALMODULIN FROM DROSOPHILA MELANOGASTER REFINED AT 2.2-ANGSTROMS RESOLUTION


Overview

The crystal structure of calmodulin (Mr 16,700, 148 residues) from Drosophila melanogaster as expressed in a bacterial system has been determined and refined at 2.2-A resolution. Starting with the structure of mammalian calmodulin, we produced an extensively refitted and refined model with a conventional crystallographic R value of 0.197 for the 5,239 reflections (F greater than or equal to 2 sigma (F)) within the 10.0-2.2-A resolution range. The model includes 1,164 protein atoms, 4 calcium ions, and 78 water molecules and has root mean square deviations from standard values of 0.018 A for bond lengths and 0.043 A for angle distances. The overall structure is similar to mammalian calmodulin, with a seven-turn central helix connecting the two calcium-binding domains. The "dumb-bell" shaped molecule contains seven alpha-helices and four "EF hand" calcium-binding sites. Although the amino acid sequences of mammalian and Drosophila calmodulins differ by only three conservative amino acid changes, the refined model reveals a number of significant differences between the two structures. Superimposition of the structures yields a root mean square deviation of 1.22 A for the 1,120 equivalent atoms. The calcium-binding domains have a root mean square deviation of 0.85 A for the 353 equivalent atoms. There are also differences in the amino terminus, the bend of the central alpha-helix, and the orientations of some of the side chains.

About this Structure

4CLN is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.

Reference

Structure of a recombinant calmodulin from Drosophila melanogaster refined at 2.2-A resolution., Taylor DA, Sack JS, Maune JF, Beckingham K, Quiocho FA, J Biol Chem. 1991 Nov 15;266(32):21375-80. PMID:1939171 Page seeded by OCA on Sun May 4 22:22:15 2008

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