2dqa

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[[Image:2dqa.jpg|left|200px]]
[[Image:2dqa.jpg|left|200px]]
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{{Structure
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|PDB= 2dqa |SIZE=350|CAPTION= <scene name='initialview01'>2dqa</scene>, resolution 1.60&Aring;
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The line below this paragraph, containing "STRUCTURE_2dqa", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|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>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|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>
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|GENE=
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{{STRUCTURE_2dqa| PDB=2dqa | SCENE= }}
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|RELATEDENTRY=
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|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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'''Crystal Structure of Tapes japonica Lysozyme'''
'''Crystal Structure of Tapes japonica Lysozyme'''
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[[Category: Takeshita, K.]]
[[Category: Takeshita, K.]]
[[Category: Ueda, T.]]
[[Category: Ueda, T.]]
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[[Category: enzyme]]
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[[Category: Enzyme]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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[[Category: lysozyme]]
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[[Category: Lysozyme]]
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[[Category: substrate complex]]
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[[Category: Substrate complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 00:57:15 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:38:00 2008''
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Revision as of 21:57, 3 May 2008

Template:STRUCTURE 2dqa

Crystal Structure of Tapes japonica Lysozyme


Overview

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 Structure

2DQA is a Single protein structure of sequence from Tapes japonica. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Sun May 4 00:57:15 2008

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