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| | ==STRUCTURAL BASIS FOR SUBSTRATE RECOGNITION BY ERWINIA CHRYSANTHEMI GH5 GLUCURONOXYLANASE== | | ==STRUCTURAL BASIS FOR SUBSTRATE RECOGNITION BY ERWINIA CHRYSANTHEMI GH5 GLUCURONOXYLANASE== |
| - | <StructureSection load='2y24' size='340' side='right' caption='[[2y24]], [[Resolution|resolution]] 1.39Å' scene=''> | + | <StructureSection load='2y24' size='340' side='right'caption='[[2y24]], [[Resolution|resolution]] 1.39Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2y24]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"erwinia_carotovora_var._chrysanthemi"_(burkholder_et_al._1953)_dye_1969 "erwinia carotovora var. chrysanthemi" (burkholder et al. 1953) dye 1969]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y24 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2Y24 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2y24]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Dickeya_chrysanthemi Dickeya chrysanthemi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y24 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y24 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=GCV:4-O-METHYL-ALPHA-D-GLUCURONIC+ACID'>GCV</scene>, <scene name='pdbligand=XYP:BETA-D-XYLOPYRANOSE'>XYP</scene></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]] 1.39Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1nof|1nof]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GCV:4-O-METHYL-ALPHA-D-GLUCURONIC+ACID'>GCV</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=XYP:BETA-D-XYLOPYRANOSE'>XYP</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2y24 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y24 OCA], [http://pdbe.org/2y24 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2y24 RCSB], [http://www.ebi.ac.uk/pdbsum/2y24 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2y24 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=2y24 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y24 OCA], [https://pdbe.org/2y24 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y24 RCSB], [https://www.ebi.ac.uk/pdbsum/2y24 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y24 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q46961_DICCH Q46961_DICCH] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Biely, P]] | + | [[Category: Dickeya chrysanthemi]] |
| - | [[Category: Hoff, T]] | + | [[Category: Large Structures]] |
| - | [[Category: Krogh, K B]] | + | [[Category: Biely P]] |
| - | [[Category: Urbanikova, L]] | + | [[Category: Hoff T]] |
| - | [[Category: Vrsanska, M]] | + | [[Category: Krogh KB]] |
| - | [[Category: Aldotetraouronic acid]] | + | [[Category: Urbanikova L]] |
| - | [[Category: Gh5 family]] | + | [[Category: Vrsanska M]] |
| - | [[Category: Glucuronoxylan-specific xylanase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
2y24 is a 1 chain structure with sequence from Dickeya chrysanthemi. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.39Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
Q46961_DICCH
Publication Abstract from PubMed
Xylanase A from the phytopathogenic bacterium Erwinia chrysanthemi is classified as a glycoside hydrolase family 30 enzyme (previously in family 5) and is specialized for degradation of glucuronoxylan. The recombinant enzyme was crystallized with the aldotetraouronic acid beta-d-xylopyranosyl-(1-->4)-[4-O-methyl-alpha-d-glucuronosyl-(1-->2)]-bet a-d-xylopyranosyl-(1-->4)-d-xylose as a ligand. The crystal structure of the enzyme-ligand complex was solved at 1.39 A resolution. The ligand xylotriose moiety occupies subsites -1, -2 and -3, whereas the methyl glucuronic acid residue attached to the middle xylopyranosyl residue of xylotriose is bound to the enzyme through hydrogen bonds to five amino acids and by the ionic interaction of the methyl glucuronic acid carboxylate with the positively charged guanidinium group of Arg293. The interaction of the enzyme with the methyl glucuronic acid residue appears to be indispensable for proper distortion of the xylan chain and its effective hydrolysis. Such a distortion does not occur with linear beta-1,4-xylooligosaccharides, which are hydrolyzed by the enzyme at a negligible rate. Database Structural and experimental data are available in the Protein Data Bank database under accession number 2y24 [45].
Structural basis for substrate recognition by Erwinia chrysanthemi GH30 glucuronoxylanase.,Urbanikova L, Vrsanska M, Morkeberg Krogh KB, Hoff T, Biely P FEBS J. 2011 Apr 19. doi: 10.1111/j.1742-4658.2011.08127.x. PMID:21501386[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Urbanikova L, Vrsanska M, Morkeberg Krogh KB, Hoff T, Biely P. Structural basis for substrate recognition by Erwinia chrysanthemi GH30 glucuronoxylanase. FEBS J. 2011 Apr 19. doi: 10.1111/j.1742-4658.2011.08127.x. PMID:21501386 doi:10.1111/j.1742-4658.2011.08127.x
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