1d6p: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
|PDB= 1d6p |SIZE=350|CAPTION= <scene name='initialview01'>1d6p</scene>, resolution 2.23Å | |PDB= 1d6p |SIZE=350|CAPTION= <scene name='initialview01'>1d6p</scene>, resolution 2.23Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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] | |ACTIVITY= <span class='plainlinks'>[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] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1rey|1REY]], [[1d6q|1D6Q]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1d6p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d6p OCA], [http://www.ebi.ac.uk/pdbsum/1d6p PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1d6p RCSB]</span> | |||
}} | }} | ||
| Line 27: | Line 30: | ||
[[Category: Sato, K.]] | [[Category: Sato, K.]] | ||
[[Category: Sugita, N.]] | [[Category: Sugita, N.]] | ||
[[Category: affinity labeling]] | [[Category: affinity labeling]] | ||
[[Category: hydrolase (o-glycosyl)]] | [[Category: hydrolase (o-glycosyl)]] | ||
[[Category: lysozyme]] | [[Category: lysozyme]] | ||
[[Category: muramidase]] | [[Category: muramidase]] | ||
[[Category: n | [[Category: n,n'-diacetylchitobiose]] | ||
[[Category: site-directed mutagenesis]] | [[Category: site-directed mutagenesis]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:35:43 2008'' | ||
Revision as of 19:35, 30 March 2008
| |||||||
| , resolution 2.23Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Lysozyme, with EC number 3.2.1.17 | ||||||
| Related: | 1REY, 1D6Q
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
Page seeded by OCA on Sun Mar 30 19:35:43 2008