1cll
From Proteopedia
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'''CALMODULIN STRUCTURE REFINED AT 1.7 ANGSTROMS RESOLUTION''' | '''CALMODULIN STRUCTURE REFINED AT 1.7 ANGSTROMS RESOLUTION''' | ||
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[[Category: Chattopadhyaya, R.]] | [[Category: Chattopadhyaya, R.]] | ||
[[Category: Quiocho, F A.]] | [[Category: Quiocho, F A.]] | ||
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| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:51:56 2008'' | |
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Revision as of 09:51, 2 May 2008
CALMODULIN STRUCTURE REFINED AT 1.7 ANGSTROMS RESOLUTION
Overview
We have determined and refined the crystal structure of a recombinant calmodulin at 1.7 A resolution. The structure was determined by molecular replacement, using the 2.2 A published native bovine brain structure as the starting model. The final crystallographic R-factor, using 14,469 reflections in the 10.0 to 1.7 A range with structure factors exceeding 0.5 sigma, is 0.216. Bond lengths and bond angle distances have root-mean-square deviations from ideal values of 0.009 A and 0.032 A, respectively. The final model consists of 1279 non-hydrogen atoms, including four calcium ions, 1130 protein atoms, including three Asp118 side-chain atoms in double conformation, 139 water molecules and one ethanol molecule. The electron densities for residues 1 to 4 and 148 of calmodulin are poorly defined, and not included in our model, except for main-chain atoms of residue 4. The calmodulin structure from our crystals is very similar to the earlier 2.2 A structure described by Babu and coworkers with a root-mean-square deviation of 0.36 A. Calmodulin remains a dumb-bell-shaped molecule, with similar lobes and connected by a central alpha-helix. Each lobe contains three alpha-helices and two Ca2+ binding EF hand loops, with a short antiparallel beta-sheet between adjacent EF hand loops and one non-EF hand loop. There are some differences in the structure of the central helix. The crystal packing is extensively studied, and facile crystal growth along the z-axis of the triclinic crystals is explained. Herein, we describe hydrogen bonding in the various secondary structure elements and hydration of calmodulin.
About this Structure
1CLL is a Single protein structure of sequence from Homo sapiens. The following page contains interesting information on the relation of 1CLL with [Calmodulin]. Full crystallographic information is available from OCA.
Reference
Calmodulin structure refined at 1.7 A resolution., Chattopadhyaya R, Meador WE, Means AR, Quiocho FA, J Mol Biol. 1992 Dec 20;228(4):1177-92. PMID:1474585 Page seeded by OCA on Fri May 2 12:51:56 2008
