2cjl: Difference between revisions

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-[[Image:2cjl.gif|left|200px]]<br /><applet load="2cjl" size="350" color="white" frame="true" align="right" spinBox="true"
-caption="2cjl, resolution 1.50&Aring;" />
-'''CRYSTAL STRUCTURE AND ENZYMATIC PROPERTIES OF A BACTERIAL FAMILY 19 CHITINASE REVEAL DIFFERENCES WITH PLANT ENZYMES'''<br />
-==Overview==
+==CRYSTAL STRUCTURE AND ENZYMATIC PROPERTIES OF A BACTERIAL FAMILY 19 CHITINASE REVEAL DIFFERENCES WITH PLANT ENZYMES==
-We describe the cloning, overexpression, purification, characterization, and crystal structure of chitinase G, a single-domain family 19 chitinase, from the Gram-positive bacterium Streptomyces coelicolor A3(2). Although, chitinase G was not capable of releasing 4-methylumbelliferyl from, artificial chitooligosaccharide substrates, it was capable of degrading, longer chitooligosaccharides at rates similar to those observed for other, chitinases. The enzyme was also capable of degrading a colored colloidal, chitin substrate (carboxymethyl-chitin-remazol-brilliant violet) and a, small, presumably amorphous, subfraction of alpha-chitin and beta-chitin, but was not capable of degrading crystalline chitin completely. The, crystal structures of chitinase G and a related Streptomyces chitinase, chitinase C [Kezuka Y, Ohishi M, Itoh Y, Watanabe J, Mitsutomi M, Watanabe, T &amp; Nonaka T (2006) J Mol Biol358, 472-484], showed that these bacterial, family 19 chitinases lack several loops that extend the substrate-binding, grooves in family 19 chitinases from plants. In accordance with these, structural features, detailed analysis of the degradation of, chitooligosaccharides by chitinase G showed that the enzyme has only four, subsites (- 2 to + 2), as opposed to six (- 3 to + 3) for plant enzymes., The most prominent structural difference leading to reduced size of the, substrate-binding groove is the deletion of a 13-residue loop between the, two putatively catalytic glutamates. The importance of these two residues, for catalysis was confirmed by a site-directed mutagenesis study.
+<StructureSection load='2cjl' size='340' side='right'caption='[[2cjl]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2cjl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CJL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CJL FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2cjl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cjl OCA], [https://pdbe.org/2cjl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cjl RCSB], [https://www.ebi.ac.uk/pdbsum/2cjl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cjl ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q8CK55_STRCO Q8CK55_STRCO]
+== 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/cj/2cjl_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=2cjl ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+We describe the cloning, overexpression, purification, characterization and crystal structure of chitinase G, a single-domain family 19 chitinase from the Gram-positive bacterium Streptomyces coelicolor A3(2). Although chitinase G was not capable of releasing 4-methylumbelliferyl from artificial chitooligosaccharide substrates, it was capable of degrading longer chitooligosaccharides at rates similar to those observed for other chitinases. The enzyme was also capable of degrading a colored colloidal chitin substrate (carboxymethyl-chitin-remazol-brilliant violet) and a small, presumably amorphous, subfraction of alpha-chitin and beta-chitin, but was not capable of degrading crystalline chitin completely. The crystal structures of chitinase G and a related Streptomyces chitinase, chitinase C [Kezuka Y, Ohishi M, Itoh Y, Watanabe J, Mitsutomi M, Watanabe T &amp; Nonaka T (2006) J Mol Biol358, 472-484], showed that these bacterial family 19 chitinases lack several loops that extend the substrate-binding grooves in family 19 chitinases from plants. In accordance with these structural features, detailed analysis of the degradation of chitooligosaccharides by chitinase G showed that the enzyme has only four subsites (- 2 to + 2), as opposed to six (- 3 to + 3) for plant enzymes. The most prominent structural difference leading to reduced size of the substrate-binding groove is the deletion of a 13-residue loop between the two putatively catalytic glutamates. The importance of these two residues for catalysis was confirmed by a site-directed mutagenesis study.
-==About this Structure==
+Crystal structure and enzymatic properties of a bacterial family 19 chitinase reveal differences from plant enzymes.,Hoell IA, Dalhus B, Heggset EB, Aspmo SI, Eijsink VG FEBS J. 2006 Nov;273(21):4889-900. Epub 2006 Sep 28. PMID:17010167<ref>PMID:17010167</ref>
-CJL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Known structural/functional Site: <scene name='pdbsite=AC1:Zn+Binding+Site+For+Chain+B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CJL OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-Crystal structure and enzymatic properties of a bacterial family 19 chitinase reveal differences from plant enzymes., Hoell IA, Dalhus B, Heggset EB, Aspmo SI, Eijsink VG, FEBS J. 2006 Nov;273(21):4889-900. Epub 2006 Sep 28. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17010167 17010167]
+</div>
-[[Category: Chitinase]]
+<div class="pdbe-citations 2cjl" style="background-color:#fffaf0;"></div>
-[[Category: Single protein]]
+==See Also==
+*[[Chitinase 3D structures|Chitinase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Streptomyces coelicolor]]
-[[Category: Aspmo, S.I.]]
+[[Category: Aspmo SI]]
-[[Category: Dalhus, B.]]
+[[Category: Dalhus B]]
-[[Category: Eijsink, V.G.H.]]
+[[Category: Eijsink VGH]]
-[[Category: Heggset, E.B.]]
+[[Category: Heggset EB]]
-[[Category: Hoell, I.A.]]
+[[Category: Hoell IA]]
-[[Category: ZN]]
-[[Category: hydrolase]]
-[[Category: plant enzymes]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:36:08 2008''