2ebs
From Proteopedia
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'''Crystal Structure Anaalysis of Oligoxyloglucan reducing-end-specific cellobiohydrolase (OXG-RCBH) D465N Mutant Complexed with a Xyloglucan Heptasaccharide''' | '''Crystal Structure Anaalysis of Oligoxyloglucan reducing-end-specific cellobiohydrolase (OXG-RCBH) D465N Mutant Complexed with a Xyloglucan Heptasaccharide''' | ||
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[[Category: Sugimoto, H.]] | [[Category: Sugimoto, H.]] | ||
[[Category: Yaoi, K.]] | [[Category: Yaoi, K.]] | ||
| - | [[Category: | + | [[Category: Beta-propeller]] |
| - | [[Category: | + | [[Category: Hydrolase]] |
| - | [[Category: | + | [[Category: National project on protein structural and functional analyse]] |
| - | [[Category: | + | [[Category: Nppsfa]] |
| - | [[Category: | + | [[Category: Riken structural genomics/proteomics initiative]] |
| - | [[Category: | + | [[Category: Rsgi]] |
| - | [[Category: | + | [[Category: Structural genomic]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 02:17:41 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 23:17, 3 May 2008
Crystal Structure Anaalysis of Oligoxyloglucan reducing-end-specific cellobiohydrolase (OXG-RCBH) D465N Mutant Complexed with a Xyloglucan Heptasaccharide
Overview
Oligoxyloglucan reducing end-specific cellobiohydrolase (OXG-RCBH) is a unique exo-beta-1,4-glucanase that belongs to glycoside hydrolase family 74. The enzyme recognizes the reducing end of xyloglucan oligosaccharides and releases two glucosyl residue segments from the reducing end of the main chain. Previously, we reported that OXG-RCBH consists of two seven-bladed beta-propeller domains. There is a large cleft between the two domains, and a unique loop encloses one side of the active site cleft. Here, we report the X-ray crystal structure of the OXG-RCBH-substrate complex determined to a resolution of 2.4 A. The substrate bound to the cleft, and its reducing end was arranged near the loop region that is believed to impart OXG-RCBH with its activity. We constructed a deletion mutant of the loop region and conducted a detailed analysis. A deletion mutant of the loop region showed endo-activity with altered substrate recognition. More specifically, cleavage occurred randomly instead of at specific sites, most likely due to the misalignment of the substrate within the subsite. We believe that the loop imparts unique substrate specificity with exo-mode hydrolysis in OXG-RCBH.
About this Structure
2EBS is a Single protein structure of sequence from Geotrichum sp. m128. Full crystallographic information is available from OCA.
Reference
The structural basis for the exo-mode of action in GH74 oligoxyloglucan reducing end-specific cellobiohydrolase., Yaoi K, Kondo H, Hiyoshi A, Noro N, Sugimoto H, Tsuda S, Mitsuishi Y, Miyazaki K, J Mol Biol. 2007 Jun 29;370(1):53-62. Epub 2007 Apr 19. PMID:17498741 Page seeded by OCA on Sun May 4 02:17:41 2008
Categories: Geotrichum sp. m128 | Oligoxyloglucan reducing-end-specific cellobiohydrolase | Single protein | Hiyoshi, A. | Kondo, H. | Miyazaki, K. | Noro, N. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Sugimoto, H. | Yaoi, K. | Beta-propeller | Hydrolase | National project on protein structural and functional analyse | Nppsfa | Riken structural genomics/proteomics initiative | Rsgi | Structural genomic
