2lhm
CRYSTAL STRUCTURES OF THE APO-AND HOLOMUTANT HUMAN LYSOZYMES WITH AN INTRODUCED CA2+ BINDING SITE
|
OverviewOverview
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.
DiseaseDisease
Known diseases associated with this structure: Amyloidosis, renal OMIM:[153450], Microphthalmia, syndromic 1 OMIM:[309800]
About this StructureAbout this Structure
2LHM is a Single protein structure of sequence from Homo sapiens. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.
ReferenceReference
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
Page seeded by OCA on Mon Nov 12 22:58:15 2007