1d6p: Difference between revisions
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[[Image:1d6p.gif|left|200px]] | [[Image:1d6p.gif|left|200px]] | ||
'''HUMAN LYSOZYME L63 MUTANT LABELLED WITH 2',3'-EPOXYPROPYL N,N'-DIACETYLCHITOBIOSE''' | {{Structure | ||
|PDB= 1d6p |SIZE=350|CAPTION= <scene name='initialview01'>1d6p</scene>, resolution 2.23Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | |||
|ACTIVITY= [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] | |||
|GENE= | |||
}} | |||
'''HUMAN LYSOZYME L63 MUTANT LABELLED WITH 2',3'-EPOXYPROPYL N,N'-DIACETYLCHITOBIOSE''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1D6P is a [ | 1D6P is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D6P OCA]. | ||
==Reference== | ==Reference== | ||
Protein-carbohydrate interactions in human lysozyme probed by combining site-directed mutagenesis and affinity labeling., Muraki M, Harata K, Sugita N, Sato KI, Biochemistry. 2000 Jan 18;39(2):292-9. PMID:[http:// | Protein-carbohydrate interactions in human lysozyme probed by combining site-directed mutagenesis and affinity labeling., Muraki M, Harata K, Sugita N, Sato KI, Biochemistry. 2000 Jan 18;39(2):292-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10630988 10630988] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Lysozyme]] | [[Category: Lysozyme]] | ||
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[[Category: site-directed mutagenesis]] | [[Category: site-directed mutagenesis]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:33:37 2008'' | ||
Revision as of 11:33, 20 March 2008
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| , resolution 2.23Å | |||||||
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| Ligands: | |||||||
| Activity: | Lysozyme, with EC number 3.2.1.17 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HUMAN LYSOZYME L63 MUTANT LABELLED WITH 2',3'-EPOXYPROPYL N,N'-DIACETYLCHITOBIOSE
OverviewOverview
The synergism between apolar and polar interactions in the carbohydrate recognition by human lysozyme (HL) was probed by site-directed mutagenesis and affinity labeling. The three-dimensional structures of the Tyr63-->Leu mutant HL labeled with 2',3'-epoxypropyl beta-glycoside of N,N'-diacetylchitobiose (L63-HL/NAG-NAG-EPO complex) and the Asp102-->Glu mutant HL labeled with the 2',3'-epoxypropyl beta-glycoside of N-acetyllactosamine were revealed by X-ray diffraction at 2.23 and 1.96 A resolution, respectively. Compared to the wild-type HL labeled with the 2', 3'-epoxypropyl beta-glycoside of N,N'-diacetylchitobiose, the N-acetylglucosamine residue at subsite B of the L63-HL/NAG-NAG-EPO complex markedly moved away from the 63rd residue, with substantial loss of hydrogen-bonding interactions. Evidently, the stacking interaction with the aromatic side chain of Tyr63 is essential in positioning the N-acetylglucosamine residue in the productive binding mode. On the other hand, the position of the galactose residue in subsite B of HL is almost unchanged by the mutation of Asp102 to Glu. Most hydrogen bonds, including the one between the carboxylate group of Glu102 and the axial 4-OH group of the galactose residue, were maintained by local movement of the backbone from residues 102-104. In both structures, the conformation of the disaccharide was conserved, reflecting an intrinsic conformational rigidity of the disaccharides. The structural analysis suggested that CH-pi interactions played an important role in the recognition of the carbohydrate residue at subsite B of HL.
About this StructureAbout this Structure
1D6P is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Protein-carbohydrate interactions in human lysozyme probed by combining site-directed mutagenesis and affinity labeling., Muraki M, Harata K, Sugita N, Sato KI, Biochemistry. 2000 Jan 18;39(2):292-9. PMID:10630988
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