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[[Image:2dbt.gif|left|200px]]


{{Structure
==Crystal structure of chitinase C from Streptomyces griseus HUT6037==
|PDB= 2dbt |SIZE=350|CAPTION= <scene name='initialview01'>2dbt</scene>, resolution 3.14&Aring;
<StructureSection load='2dbt' size='340' side='right'caption='[[2dbt]], [[Resolution|resolution]] 3.14&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>
<table><tr><td colspan='2'>[[2dbt]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_griseus Streptomyces griseus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DBT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DBT FirstGlance]. <br>
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Chitinase Chitinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.14 3.2.1.14] </span>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.14&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2dbt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dbt OCA], [https://pdbe.org/2dbt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dbt RCSB], [https://www.ebi.ac.uk/pdbsum/2dbt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dbt ProSAT]</span></td></tr>
|RELATEDENTRY=[[1wvu|1WVU]], [[1wvv|1WVV]]
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2dbt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dbt OCA], [http://www.ebi.ac.uk/pdbsum/2dbt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2dbt RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/O50152_STRGR O50152_STRGR]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/db/2dbt_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2dbt ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Chitinase C (ChiC) from Streptomyces griseus HUT6037 was the first glycoside hydrolase family 19 chitinase that was found in an organism other than higher plants. An N-terminal chitin-binding domain and a C-terminal catalytic domain connected by a linker peptide constitute ChiC. We determined the crystal structure of full-length ChiC, which is the only representative of the two-domain chitinases in the family. The catalytic domain has an alpha-helix-rich fold with a deep cleft containing a catalytic site, and lacks three loops on the domain surface compared with the catalytic domain of plant chitinases. The chitin-binding domain is an all-beta protein with two tryptophan residues (Trp59 and Trp60) aligned on the surface. We suggest the binding mechanism of tri-N-acetylchitotriose onto the chitin-binding domain on the basis of molecular dynamics (MD) simulations. In this mechanism, the ligand molecule binds well on the surface-exposed binding site through two stacking interactions and two hydrogen bonds and only Trp59 and Trp60 are involved in the binding. Furthermore, the flexibility of the Trp60 side-chain, which may be involved in adjusting the binding surface to fit the surface of crystalline chitin by the rotation of chi2 angle, is shown.


'''Crystal structure of chitinase C from Streptomyces griseus HUT6037'''
Structural studies of a two-domain chitinase from Streptomyces griseus HUT6037.,Kezuka Y, Ohishi M, Itoh Y, Watanabe J, Mitsutomi M, Watanabe T, Nonaka T J Mol Biol. 2006 Apr 28;358(2):472-84. Epub 2006 Feb 21. PMID:16516924<ref>PMID:16516924</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2dbt" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
Chitinase C (ChiC) from Streptomyces griseus HUT6037 was the first glycoside hydrolase family 19 chitinase that was found in an organism other than higher plants. An N-terminal chitin-binding domain and a C-terminal catalytic domain connected by a linker peptide constitute ChiC. We determined the crystal structure of full-length ChiC, which is the only representative of the two-domain chitinases in the family. The catalytic domain has an alpha-helix-rich fold with a deep cleft containing a catalytic site, and lacks three loops on the domain surface compared with the catalytic domain of plant chitinases. The chitin-binding domain is an all-beta protein with two tryptophan residues (Trp59 and Trp60) aligned on the surface. We suggest the binding mechanism of tri-N-acetylchitotriose onto the chitin-binding domain on the basis of molecular dynamics (MD) simulations. In this mechanism, the ligand molecule binds well on the surface-exposed binding site through two stacking interactions and two hydrogen bonds and only Trp59 and Trp60 are involved in the binding. Furthermore, the flexibility of the Trp60 side-chain, which may be involved in adjusting the binding surface to fit the surface of crystalline chitin by the rotation of chi2 angle, is shown.
*[[Chitinase 3D structures|Chitinase 3D structures]]
 
== References ==
==About this Structure==
<references/>
2DBT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_griseus Streptomyces griseus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DBT OCA].
__TOC__
 
</StructureSection>
==Reference==
[[Category: Large Structures]]
Structural studies of a two-domain chitinase from Streptomyces griseus HUT6037., Kezuka Y, Ohishi M, Itoh Y, Watanabe J, Mitsutomi M, Watanabe T, Nonaka T, J Mol Biol. 2006 Apr 28;358(2):472-84. Epub 2006 Feb 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16516924 16516924]
[[Category: Chitinase]]
[[Category: Single protein]]
[[Category: Streptomyces griseus]]
[[Category: Streptomyces griseus]]
[[Category: Kezuka, Y.]]
[[Category: Kezuka Y]]
[[Category: Nonaka, T.]]
[[Category: Nonaka T]]
[[Category: Watanabe, T.]]
[[Category: Watanabe T]]
[[Category: family 19 chitinase]]
 
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