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==Crystal Structure of a Family GH19 chitinase from Bryum coronatum in complex with (GlcNAc)4== | ==Crystal Structure of a Family GH19 chitinase from Bryum coronatum in complex with (GlcNAc)4== | ||
<StructureSection load='4ij4' size='340' side='right'caption='[[4ij4]]' scene=''> | <StructureSection load='4ij4' size='340' side='right'caption='[[4ij4]], [[Resolution|resolution]] 1.58Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IJ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IJ4 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4ij4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gemmabryum_coronatum Gemmabryum coronatum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IJ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IJ4 FirstGlance]. <br> | ||
</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=4ij4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ij4 OCA], [https://pdbe.org/4ij4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ij4 RCSB], [https://www.ebi.ac.uk/pdbsum/4ij4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ij4 ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.58Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=4ij4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ij4 OCA], [https://pdbe.org/4ij4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ij4 RCSB], [https://www.ebi.ac.uk/pdbsum/4ij4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ij4 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A9ZSX9_9BRYO A9ZSX9_9BRYO] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
DESCRIPTIONS: The structure of a GH19 chitinase from the moss Bryum coronatum (BcChi-A) in complex with the substrate was examined by X-ray crystallography and NMR spectroscopy in solution. The X-ray crystal structure of the inactive mutant of BcChi-A (BcChi-A-E61A) liganded with chitin tetramer (GlcNAc)4 revealed a clear electron density of the tetramer bound to subsites -2, -1, +1, and +2. Individual sugar residues were recognized by several amino acids at these subsites through a number of hydrogen bonds. This is the first crystal structure of GH19 chitinase liganded with oligosaccharide spanning the catalytic center. NMR titration experiments of chitin oligosaccharides into the BcChi-A-E61A solution showed that the binding mode observed in the crystal structure is similar to that in solution. The C-1 carbon of -1 GlcNAc, the Oepsilon1 atom of the catalytic base (Glu70), and the Ogamma atom of Ser102 form a "triangle" surrounding the catalytic water, and the arrangement structurally validated the proposed catalytic mechanism of GH19 chitinases. The glycosidic linkage between -1 and +1 sugars was found to be twisted and under strain. This situation may contribute to the reduction of activation energy for hydrolysis. The complex structure revealed a more refined mechanism of the chitinase catalysis. | |||
Crystal structure of a "loopless" GH19 chitinase in complex with chitin tetrasaccharide spanning the catalytic center.,Ohnuma T, Umemoto N, Nagata T, Shinya S, Numata T, Taira T, Fukamizo T Biochim Biophys Acta. 2014 Feb 25;1844(4):793-802. doi:, 10.1016/j.bbapap.2014.02.013. PMID:24582745<ref>PMID:24582745</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4ij4" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Chitinase 3D structures|Chitinase 3D structures]] | *[[Chitinase 3D structures|Chitinase 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Gemmabryum coronatum]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Fukamizo T]] | [[Category: Fukamizo T]] | ||
Latest revision as of 13:58, 6 November 2024
Crystal Structure of a Family GH19 chitinase from Bryum coronatum in complex with (GlcNAc)4Crystal Structure of a Family GH19 chitinase from Bryum coronatum in complex with (GlcNAc)4
Structural highlights
FunctionPublication Abstract from PubMedDESCRIPTIONS: The structure of a GH19 chitinase from the moss Bryum coronatum (BcChi-A) in complex with the substrate was examined by X-ray crystallography and NMR spectroscopy in solution. The X-ray crystal structure of the inactive mutant of BcChi-A (BcChi-A-E61A) liganded with chitin tetramer (GlcNAc)4 revealed a clear electron density of the tetramer bound to subsites -2, -1, +1, and +2. Individual sugar residues were recognized by several amino acids at these subsites through a number of hydrogen bonds. This is the first crystal structure of GH19 chitinase liganded with oligosaccharide spanning the catalytic center. NMR titration experiments of chitin oligosaccharides into the BcChi-A-E61A solution showed that the binding mode observed in the crystal structure is similar to that in solution. The C-1 carbon of -1 GlcNAc, the Oepsilon1 atom of the catalytic base (Glu70), and the Ogamma atom of Ser102 form a "triangle" surrounding the catalytic water, and the arrangement structurally validated the proposed catalytic mechanism of GH19 chitinases. The glycosidic linkage between -1 and +1 sugars was found to be twisted and under strain. This situation may contribute to the reduction of activation energy for hydrolysis. The complex structure revealed a more refined mechanism of the chitinase catalysis. Crystal structure of a "loopless" GH19 chitinase in complex with chitin tetrasaccharide spanning the catalytic center.,Ohnuma T, Umemoto N, Nagata T, Shinya S, Numata T, Taira T, Fukamizo T Biochim Biophys Acta. 2014 Feb 25;1844(4):793-802. doi:, 10.1016/j.bbapap.2014.02.013. PMID:24582745[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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