Structural highlights
1qnr is a 1 chain structure with sequence from Trichoderma reesei. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Method: | X-ray diffraction, Resolution 1.4Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
MANA_HYPJR Endo-1,4-mannanase that catalyzes the random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans and heteromannans. It is a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans. Active against locust bean gum and ivory nut mannan, releasing mainly tri- and disaccharides (PubMed:7793911, PubMed:8529653, Ref.3, Ref.4). Also has transglycosylation activity. Transglycosylation of two mannotrioses into a mannohexaose is the major transglycosylation route (PubMed:24950755, PubMed:8529653, Ref.7).[1] [2] [3] [PROSITE-ProRule:PRU00597][SAM:MobiDB-lite][4]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The crystal structure of the catalytic core domain of beta-mannanase from the fungus Trichoderma reesei has been determined at a resolution of 1.5 A. The structure was solved using the anomalous scattering from a single non-isomorphous platinum complex with two heavy-metal sites in space group P2(1). The map computed with the experimental phases was enhanced by the application of an automated model building and refinement procedure using the amplitudes and experimental phases as observations. This approach is expected to be of more general application. The structure of the native enzyme and complexes with Tris-HCl and mannobiose are also reported: the mannobiose binds in subsites +1 and +2. The structure is briefly compared with that of the homologous beta-mannanase from the bacterium Thermomonospora fusca.
The three-dimensional structure of a Trichoderma reesei beta-mannanase from glycoside hydrolase family 5.,Sabini E, Schubert H, Murshudov G, Wilson KS, Siika-Aho M, Penttila M Acta Crystallogr D Biol Crystallogr. 2000 Jan;56(Pt 1):3-13. PMID:10666621[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Rosengren A, Reddy SK, Sjöberg JS, Aurelius O, Logan DT, Kolenová K, Stålbrand H. An Aspergillus nidulans β-mannanase with high transglycosylation capacity revealed through comparative studies within glycosidase family 5. Appl Microbiol Biotechnol. 2014 Dec;98(24):10091-104. PMID:24950755 doi:10.1007/s00253-014-5871-8
- ↑ Stålbrand H, Saloheimo A, Vehmaanperä J, Henrissat B, Penttilä M. Cloning and expression in Saccharomyces cerevisiae of a Trichoderma reesei beta-mannanase gene containing a cellulose binding domain. Appl Environ Microbiol. 1995 Mar;61(3):1090-7. PMID:7793911 doi:10.1128/aem.61.3.1090-1097.1995
- ↑ Harjunpää V, Teleman A, Siika-Aho M, Drakenberg T. Kinetic and stereochemical studies of manno-oligosaccharide hydrolysis catalysed by beta-mannanases from Trichoderma reesei. Eur J Biochem. 1995 Nov 15;234(1):278-83. PMID:8529653 doi:10.1111/j.1432-1033.1995.278_c.x
- ↑ Rosengren A, Reddy SK, Sjöberg JS, Aurelius O, Logan DT, Kolenová K, Stålbrand H. An Aspergillus nidulans β-mannanase with high transglycosylation capacity revealed through comparative studies within glycosidase family 5. Appl Microbiol Biotechnol. 2014 Dec;98(24):10091-104. PMID:24950755 doi:10.1007/s00253-014-5871-8
- ↑ Sabini E, Schubert H, Murshudov G, Wilson KS, Siika-Aho M, Penttila M. The three-dimensional structure of a Trichoderma reesei beta-mannanase from glycoside hydrolase family 5. Acta Crystallogr D Biol Crystallogr. 2000 Jan;56(Pt 1):3-13. PMID:10666621
