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| | <StructureSection load='2z37' size='340' side='right'caption='[[2z37]], [[Resolution|resolution]] 1.53Å' scene=''> | | <StructureSection load='2z37' size='340' side='right'caption='[[2z37]], [[Resolution|resolution]] 1.53Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2z37]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Braju Braju]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z37 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Z37 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2z37]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Brassica_juncea Brassica juncea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z37 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Z37 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2z38|2z38]], [[2z39|2z39]]</div></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]] 1.53Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Bjchi1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3707 BRAJU])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Chitinase Chitinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.14 3.2.1.14] </span></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=2z37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z37 OCA], [https://pdbe.org/2z37 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2z37 RCSB], [https://www.ebi.ac.uk/pdbsum/2z37 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2z37 ProSAT]</span></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=2z37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z37 OCA], [https://pdbe.org/2z37 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2z37 RCSB], [https://www.ebi.ac.uk/pdbsum/2z37 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2z37 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9SQF7_BRAJU Q9SQF7_BRAJU] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Braju]] | + | [[Category: Brassica juncea]] |
| - | [[Category: Chitinase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bergfors, T]] | + | [[Category: Bergfors T]] |
| - | [[Category: Berglund, G]] | + | [[Category: Berglund G]] |
| - | [[Category: Mowbray, S L]] | + | [[Category: Mowbray SL]] |
| - | [[Category: Ubhayasekera, W]] | + | [[Category: Ubhayasekera W]] |
| - | [[Category: Conformational change]]
| + | |
| - | [[Category: Endochitinase]]
| + | |
| - | [[Category: Family 19]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
Q9SQF7_BRAJU
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Brassica juncea chitinase is an endo-acting, pathogenesis-related protein that is classified into glycoside hydrolase family 19, with highest homology (50-60%) in its catalytic domain to class I plant chitinases. Here we report X-ray structures of the chitinase catalytic domain from wild-type (apo, as well as with chloride ions bound) and a Glu234Ala mutant enzyme, solved by molecular replacement and refined at 1.53, 1.8 and 1.7 A resolution, respectively. Confirming our earlier mutagenesis studies, the active-site residues are identified as Glu212 and Glu234. Glu212 is believed to be the catalytic acid in the reaction, whereas Glu234 is thought to have a dual role, both activating a water molecule in its attack on the anomeric carbon, and stabilizing the charged intermediate. The molecules in the various structures differ significantly in the conformation of a number of loops that border the active-site cleft. The differences suggest an opening and closing of the enzyme during the catalytic cycle. Chitin is expected to dock first near Glu212, which will protonate it. Conformational changes then bring Glu234 closer, allowing it to assist in the following steps. These observations provide important insights into catalysis in family 19 chitinases.
Crystal structures of a family 19 chitinase from Brassica juncea show flexibility of binding cleft loops.,Ubhayasekera W, Tang CM, Ho SW, Berglund G, Bergfors T, Chye ML, Mowbray SL FEBS J. 2007 Jul;274(14):3695-703. Epub 2007 Jul 2. PMID:17608716[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ubhayasekera W, Tang CM, Ho SW, Berglund G, Bergfors T, Chye ML, Mowbray SL. Crystal structures of a family 19 chitinase from Brassica juncea show flexibility of binding cleft loops. FEBS J. 2007 Jul;274(14):3695-703. Epub 2007 Jul 2. PMID:17608716 doi:10.1111/j.1742-4658.2007.05906.x
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