3lhm
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(New page: 200px<br /> <applet load="3lhm" size="450" color="white" frame="true" align="right" spinBox="true" caption="3lhm, resolution 1.8Å" /> '''CRYSTAL STRUCTURES O...)
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Revision as of 21:42, 12 November 2007
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CRYSTAL STRUCTURES OF THE APO-AND HOLOMUTANT HUMAN LYSOZYMES WITH AN INTRODUCED CA2+ BINDING SITE
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Overview
The three-dimensional structures of apo- and holomutant human lysozymes, (D86/92 lysozyme), in which a calcium binding site was designed and, created for enhancing molecular stability by replacing both Gln86 and, Ala92 with aspartic acids, were refined at 1.8-A resolution by x-ray, crystallography. The overall structures and crystallographic thermal, factors of all three proteins, the apo-, holo-D86/92, and the wild-type, human lysozymes, were essentially identical; these results showed that the, introduction of the calcium binding site did not affect either the overall, structure or molecular rigidity of the proteins. However, structure, analyses of the apo-D86/92 lysozyme revealed that the mutations affected, the side chain conformation of residue 86 and hydrogen networks between, the protein and the internal solvent molecules. In the structure of the, holo-D86/92 lysozyme, seven oxygen ligands formed a slightly distorted, pentagonal bipyramid around the calcium ion, indicating that the, coordination around the calcium ion was quite similar to that in baboon, alpha-lactalbumin. The pentagonal bipyramid coordination could be one of, the most widely found and appropriate calcium binding schemes in proteins.
Disease
Known diseases associated with this structure: Amyloidosis, renal OMIM:[153450], Microphthalmia, syndromic 1 OMIM:[309800]
About this Structure
3LHM is a Single protein structure of sequence from Homo sapiens with CA as ligand. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.
Reference
Crystal structures of the apo- and holomutant human lysozymes with an introduced Ca2+ binding site., Inaka K, Kuroki R, Kikuchi M, Matsushima M, J Biol Chem. 1991 Nov 5;266(31):20666-71. PMID:1939116
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