1jef
From Proteopedia
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|PDB= 1jef |SIZE=350|CAPTION= <scene name='initialview01'>1jef</scene>, resolution 1.77Å | |PDB= 1jef |SIZE=350|CAPTION= <scene name='initialview01'>1jef</scene>, resolution 1.77Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jef FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jef OCA], [http://www.ebi.ac.uk/pdbsum/1jef PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jef RCSB]</span> | ||
}} | }} | ||
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[[Category: Harata, K.]] | [[Category: Harata, K.]] | ||
[[Category: Muraki, M.]] | [[Category: Muraki, M.]] | ||
| - | [[Category: SO4]] | ||
[[Category: bacteriolytic enzyme]] | [[Category: bacteriolytic enzyme]] | ||
[[Category: enzyme]] | [[Category: enzyme]] | ||
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[[Category: inhibitor complex]] | [[Category: inhibitor complex]] | ||
| - | ''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 21:32:29 2008'' |
Revision as of 18:32, 30 March 2008
| |||||||
| , resolution 1.77Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Lysozyme, with EC number 3.2.1.17 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
TURKEY LYSOZYME COMPLEX WITH (GLCNAC)3
Overview
The turkey-egg lysozyme (TEL) complex with tri-N-acetylchitotriose [(GlcNac)3] was co-crystallized from 1.5% TEL and 2 mM (GlcNac)3 at pH 4.2. The crystal structure was determined by molecular replacement and refined to an R value of 0.182 using 10-1.77 A data. The (GlcNac)3 molecule occupies the subsites A, B and C. At the subsites B and C, the sugar residues are bound in a similar manner to that found in the hen-egg lysozyme (HEL) complex. In contrast, the GlcNac residue at the subsite A is exposed to bulk solvent and has no contact with the protein molecule because the active residue Asp101 in HEL is replaced by Gly in TEL. A sulfate ion is bound in the vicinity of subsite B and forms hydrogen bonds with the sugar residue and the guanidino group of Arg61, assisting the binding of the sugar residue to subsite B. The active-site cleft of TEL is narrower than that of native TEL, thus attaining the best fit of the (GlcNac)3 molecule. The lack of binding ability of subsite A is discussed in relation to the catalytic properties of TEL. The result suggests that the cleavage pattern of oligosaccharide substrates in the catalytic reaction is regulated by the protein-sugar interaction at subsite A.
About this Structure
1JEF is a Single protein structure of sequence from Meleagris gallopavo. Full crystallographic information is available from OCA.
Reference
X-ray structure of turkey-egg lysozyme complex with tri-N-acetylchitotriose. Lack of binding ability at subsite A., Harata K, Muraki M, Acta Crystallogr D Biol Crystallogr. 1997 Nov 1;53(Pt 6):650-7. PMID:15299852
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