2dqa

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[[Image:2dqa.jpg|left|200px]]<br /><applet load="2dqa" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2dqa.jpg|left|200px]]
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caption="2dqa, resolution 1.60&Aring;" />
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'''Crystal Structure of Tapes japonica Lysozyme'''<br />
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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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|SITE=
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|LIGAND= <scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene> and <scene name='pdbligand=PT:PLATINUM (II) ION'>PT</scene>
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|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]
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|GENE=
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}}
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'''Crystal Structure of Tapes japonica Lysozyme'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2DQA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Tapes_japonica Tapes japonica] with <scene name='pdbligand=BGC:'>BGC</scene> and <scene name='pdbligand=PT:'>PT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DQA OCA].
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2DQA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Tapes_japonica Tapes japonica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DQA OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17631496 17631496]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/17631496 17631496]
[[Category: Lysozyme]]
[[Category: Lysozyme]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: substrate complex]]
[[Category: substrate complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:01:31 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:30:11 2008''

Revision as of 14:30, 20 March 2008

Image:2dqa.jpg


PDB ID 2dqa

Drag the structure with the mouse to rotate
, resolution 1.60Å
Ligands: and
Activity: Lysozyme, with EC number 3.2.1.17
Coordinates: save as pdb, mmCIF, xml



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

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