5xyh
From Proteopedia
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- | '''Unreleased structure''' | ||
- | + | ==Crystal Structure of catalytic domain of 1,4-beta-Cellobiosidase (CbsA) from Xanthomonas oryzae pv. oryzae== | |
+ | <StructureSection load='5xyh' size='340' side='right' caption='[[5xyh]], [[Resolution|resolution]] 1.86Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[5xyh]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XYH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XYH FirstGlance]. <br> | ||
+ | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellulose_1,4-beta-cellobiosidase_(non-reducing_end) Cellulose 1,4-beta-cellobiosidase (non-reducing end)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.91 3.2.1.91] </span></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=5xyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xyh OCA], [http://pdbe.org/5xyh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xyh RCSB], [http://www.ebi.ac.uk/pdbsum/5xyh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xyh ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Xanthomonas oryzae pv. oryzae (Xoo) causes bacterial blight, a serious disease of rice. Xoo secretes a repertoire of cell wall-degrading enzymes, including cellulases, xylanases and pectinases, to degrade various polysaccharide components of the rice cell wall. A secreted Xoo cellulase, CbsA, is not only a key virulence factor of Xoo, but is also a potent inducer of innate immune responses of rice. In this study, we solved the crystal structure of the catalytic domain of the CbsA protein to a resolution of 1.86 A. The core structure of CbsA shows a central distorted TIM barrel made up of eight beta strands with N- and C-terminal loops enclosing the active site, which is a characteristic structural feature of an exoglucanase. The aspartic acid at the 131st position of CbsA was predicted to be important for catalysis and was therefore mutated to alanine to study its role in the catalysis and biological functions of CbsA. Intriguingly, the D131A CbsA mutant protein displayed the enzymatic activity of a typical endoglucanase. D131A CbsA was as proficient as wild-type (Wt) CbsA in inducing rice immune responses, but was deficient in virulence-promoting activity. This indicates that the specific exoglucanase activity of the Wt CbsA protein is required for this protein to promote the growth of Xoo in rice. | ||
- | + | A mutation in an exoglucanase of Xanthomonas oryzae pv. oryzae, which confers an endo mode of activity, affects bacterial virulence, but not the induction of immune responses, in rice.,Tayi L, Kumar S, Nathawat R, Haque AS, Maku RV, Patel HK, Sankaranarayanan R, Sonti RV Mol Plant Pathol. 2018 Jun;19(6):1364-1376. doi: 10.1111/mpp.12620. Epub 2017 Dec, 26. PMID:28976110<ref>PMID:28976110</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
+ | <div class="pdbe-citations 5xyh" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Haque, A S]] | ||
+ | [[Category: Kumar, S]] | ||
+ | [[Category: Nathawat, R]] | ||
+ | [[Category: Sankaranaryanan, R]] | ||
+ | [[Category: Bacterial blight]] | ||
+ | [[Category: Cell-wall degrading enzyme]] | ||
+ | [[Category: Exoglucanase]] | ||
+ | [[Category: Hydrolase]] | ||
+ | [[Category: Xoo]] |
Revision as of 05:26, 16 May 2018
Crystal Structure of catalytic domain of 1,4-beta-Cellobiosidase (CbsA) from Xanthomonas oryzae pv. oryzae
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