1j9y: Difference between revisions
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'''Crystal structure of mannanase 26A from Pseudomonas cellulosa''' | {{Structure | ||
|PDB= 1j9y |SIZE=350|CAPTION= <scene name='initialview01'>1j9y</scene>, resolution 1.85Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Mannan_endo-1,4-beta-mannosidase Mannan endo-1,4-beta-mannosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.78 3.2.1.78] | |||
|GENE= Man26A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=155077 Cellvibrio japonicus]) | |||
}} | |||
'''Crystal structure of mannanase 26A from Pseudomonas cellulosa''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1J9Y is a [ | 1J9Y is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Cellvibrio_japonicus Cellvibrio japonicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J9Y OCA]. | ||
==Reference== | ==Reference== | ||
Crystal structure of mannanase 26A from Pseudomonas cellulosa and analysis of residues involved in substrate binding., Hogg D, Woo EJ, Bolam DN, McKie VA, Gilbert HJ, Pickersgill RW, J Biol Chem. 2001 Aug 17;276(33):31186-92. Epub 2001 May 29. PMID:[http:// | Crystal structure of mannanase 26A from Pseudomonas cellulosa and analysis of residues involved in substrate binding., Hogg D, Woo EJ, Bolam DN, McKie VA, Gilbert HJ, Pickersgill RW, J Biol Chem. 2001 Aug 17;276(33):31186-92. Epub 2001 May 29. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11382747 11382747] | ||
[[Category: Cellvibrio japonicus]] | [[Category: Cellvibrio japonicus]] | ||
[[Category: Mannan endo-1,4-beta-mannosidase]] | [[Category: Mannan endo-1,4-beta-mannosidase]] | ||
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[[Category: Woo, E J.]] | [[Category: Woo, E J.]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: 4/7-superfamily of glycoside | [[Category: 4/7-superfamily of glycoside hydrolase]] | ||
[[Category: beta/alpha barrel]] | [[Category: beta/alpha barrel]] | ||
[[Category: clan gh-a]] | [[Category: clan gh-a]] | ||
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[[Category: tim barrel]] | [[Category: tim barrel]] | ||
''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 12:00:36 2008'' |
Revision as of 13:00, 20 March 2008
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, resolution 1.85Å | |||||||
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Ligands: | |||||||
Gene: | Man26A (Cellvibrio japonicus) | ||||||
Activity: | Mannan endo-1,4-beta-mannosidase, with EC number 3.2.1.78 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Crystal structure of mannanase 26A from Pseudomonas cellulosa
OverviewOverview
The crystal structure of Pseudomonas cellulosa mannanase 26A has been solved by multiple isomorphous replacement and refined at 1.85 A resolution to an R-factor of 0.182 (R-free = 0.211). The enzyme comprises (beta/alpha)(8)-barrel architecture with two catalytic glutamates at the ends of beta-strands 4 and 7 in precisely the same location as the corresponding glutamates in other 4/7-superfamily glycoside hydrolase enzymes (clan GH-A glycoside hydrolases). The family 26 glycoside hydrolases are therefore members of clan GH-A. Functional analyses of mannanase 26A, informed by the crystal structure of the enzyme, provided important insights into the role of residues close to the catalytic glutamates. These data showed that Trp-360 played a critical role in binding substrate at the -1 subsite, whereas Tyr-285 was important to the function of the nucleophile catalyst. His-211 in mannanase 26A does not have the same function as the equivalent asparagine in the other GH-A enzymes. The data also suggest that Trp-217 and Trp-162 are important for the activity of mannanase 26A against mannooligosaccharides but are less important for activity against polysaccharides.
About this StructureAbout this Structure
1J9Y is a Single protein structure of sequence from Cellvibrio japonicus. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of mannanase 26A from Pseudomonas cellulosa and analysis of residues involved in substrate binding., Hogg D, Woo EJ, Bolam DN, McKie VA, Gilbert HJ, Pickersgill RW, J Biol Chem. 2001 Aug 17;276(33):31186-92. Epub 2001 May 29. PMID:11382747
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