2lhm: Difference between revisions

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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.

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==

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[[Category: hydrolase (o-glycosyl)]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:07:08 2008''

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@@ Line 4: / Line 4: @@
 ==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.
+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==
@@ Line 21: / Line 21: @@
 [[Category: hydrolase (o-glycosyl)]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:37:46 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:07:08 2008''