2ebs
From Proteopedia
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| - | [[Image:2ebs.gif|left|200px]] | + | [[Image:2ebs.gif|left|200px]] |
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| - | '''Crystal Structure Anaalysis of Oligoxyloglucan reducing-end-specific cellobiohydrolase (OXG-RCBH) D465N Mutant Complexed with a Xyloglucan Heptasaccharide''' | + | {{Structure |
| + | |PDB= 2ebs |SIZE=350|CAPTION= <scene name='initialview01'>2ebs</scene>, resolution 2.40Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Oligoxyloglucan_reducing-end-specific_cellobiohydrolase Oligoxyloglucan reducing-end-specific cellobiohydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.150 3.2.1.150] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal Structure Anaalysis of Oligoxyloglucan reducing-end-specific cellobiohydrolase (OXG-RCBH) D465N Mutant Complexed with a Xyloglucan Heptasaccharide''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2EBS is a [ | + | 2EBS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Geotrichum_sp._m128 Geotrichum sp. m128]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EBS OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17498741 17498741] |
[[Category: Geotrichum sp. m128]] | [[Category: Geotrichum sp. m128]] | ||
[[Category: Oligoxyloglucan reducing-end-specific cellobiohydrolase]] | [[Category: Oligoxyloglucan reducing-end-specific cellobiohydrolase]] | ||
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[[Category: beta-propeller]] | [[Category: beta-propeller]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | [[Category: national project on protein structural and functional | + | [[Category: national project on protein structural and functional analyse]] |
[[Category: nppsfa]] | [[Category: nppsfa]] | ||
[[Category: riken structural genomics/proteomics initiative]] | [[Category: riken structural genomics/proteomics initiative]] | ||
[[Category: rsgi]] | [[Category: rsgi]] | ||
| - | [[Category: structural | + | [[Category: structural genomic]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:37:58 2008'' |
Revision as of 14:37, 20 March 2008
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| , resolution 2.40Å | |||||||
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| Activity: | Oligoxyloglucan reducing-end-specific cellobiohydrolase, with EC number 3.2.1.150 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Thu Mar 20 16:37:58 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
