2lhm
From Proteopedia
(New page: 200px<br /> <applet load="2lhm" size="450" color="white" frame="true" align="right" spinBox="true" caption="2lhm, resolution 1.8Å" /> '''CRYSTAL STRUCTURES O...) |
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caption="2lhm, resolution 1.8Å" /> | caption="2lhm, resolution 1.8Å" /> | ||
'''CRYSTAL STRUCTURES OF THE APO-AND HOLOMUTANT HUMAN LYSOZYMES WITH AN INTRODUCED CA2+ BINDING SITE'''<br /> | '''CRYSTAL STRUCTURES OF THE APO-AND HOLOMUTANT HUMAN LYSOZYMES WITH AN INTRODUCED CA2+ BINDING SITE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2LHM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http:// | + | 2LHM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LHM OCA]. |
==Reference== | ==Reference== | ||
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[[Category: hydrolase (o-glycosyl)]] | [[Category: hydrolase (o-glycosyl)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:37:46 2008'' |
Revision as of 15:37, 15 February 2008
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CRYSTAL STRUCTURES OF THE APO-AND HOLOMUTANT HUMAN LYSOZYMES WITH AN INTRODUCED CA2+ BINDING SITE
Contents |
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
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.
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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