2dqa: Difference between revisions
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|PDB= 2dqa |SIZE=350|CAPTION= <scene name='initialview01'>2dqa</scene>, resolution 1.60Å | |PDB= 2dqa |SIZE=350|CAPTION= <scene name='initialview01'>2dqa</scene>, resolution 1.60Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene> | |LIGAND= <scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PT:PLATINUM+(II)+ION'>PT</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=2dqa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dqa OCA], [http://www.ebi.ac.uk/pdbsum/2dqa PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2dqa RCSB]</span> | |||
}} | }} | ||
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[[Category: Takeshita, K.]] | [[Category: Takeshita, K.]] | ||
[[Category: Ueda, T.]] | [[Category: Ueda, T.]] | ||
[[Category: enzyme]] | [[Category: enzyme]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
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[[Category: substrate complex]] | [[Category: substrate complex]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:38:00 2008'' | ||
Revision as of 02:38, 31 March 2008
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| , resolution 1.60Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Activity: | Lysozyme, with EC number 3.2.1.17 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of Tapes japonica Lysozyme
OverviewOverview
Tapes japonica lysozyme (TJL) is classified as a member of the recently established i-type lysozyme family. In this study, we solved the crystal structure of TJL complexed with a trimer of N-acetylglucosamine to 1.6A resolution. Based on structure and mutation analyses, we demonstrated that Glu-18 and Asp-30 are the catalytic residues of TJL. Furthermore, the present findings suggest that the catalytic mechanism of TJL is a retaining mechanism that proceeds through a covalent sugar-enzyme intermediate. On the other hand, the quaternary structure in the crystal revealed a dimer formed by the electrostatic interactions of catalytic residues (Glu-18 and Asp-30) in one molecule with the positive residues at the C terminus in helix 6 of the other molecule. Gel chromatography analysis revealed that the TJL dimer remained intact under low salt conditions but that it dissociated to TJL monomers under high salt conditions. With increasing salt concentrations, the chitinase activity of TJL dramatically increased. Therefore, this study provides novel evidence that the lysozyme activity of TJL is modulated by its quaternary structure.
About this StructureAbout this Structure
2DQA is a Single protein structure of sequence from Tapes japonica. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of Tapes japonica Lysozyme with substrate analogue: structural basis of the catalytic mechanism and manifestation of its chitinase activity accompanied by quaternary structural change., Goto T, Abe Y, Kakuta Y, Takeshita K, Imoto T, Ueda T, J Biol Chem. 2007 Sep 14;282(37):27459-67. Epub 2007 Jul 13. PMID:17631496
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