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- | [[Image:1qnq.gif|left|200px]] | |
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- | <!--
| + | ==The 3-D structure of a Trichoderma reesei b-mannanase from glycoside hydrolase family 5== |
- | The line below this paragraph, containing "STRUCTURE_1qnq", creates the "Structure Box" on the page.
| + | <StructureSection load='1qnq' size='340' side='right'caption='[[1qnq]], [[Resolution|resolution]] 1.65Å' scene=''> |
- | You may change the PDB parameter (which sets the PDB file loaded into the applet)
| + | == Structural highlights == |
- | or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
| + | <table><tr><td colspan='2'>[[1qnq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trichoderma_reesei Trichoderma reesei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QNQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QNQ FirstGlance]. <br> |
- | or leave the SCENE parameter empty for the default display.
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65Å</td></tr> |
- | --> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TPT:2,2 6,2-TERPYRIDINE+PLATINUM(II)+CHLORIDE'>TPT</scene></td></tr> |
- | {{STRUCTURE_1qnq| PDB=1qnq | SCENE= }}
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qnq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qnq OCA], [https://pdbe.org/1qnq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qnq RCSB], [https://www.ebi.ac.uk/pdbsum/1qnq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qnq ProSAT]</span></td></tr> |
| + | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/MANA_HYPJR 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, Ref.3, Ref.4, PubMed:8529653). Also has transglycosylation activity. Transglycosylation of two mannotrioses into a mannohexaose is the major transglycosylation route (PubMed:8529653, Ref.7, PubMed:24950755).<ref>PMID:24950755</ref> <ref>PMID:7793911</ref> <ref>PMID:8529653</ref> [PROSITE-ProRule:PRU00597][SAM:MobiDB-lite]<ref>PMID:24950755</ref> |
| + | == Evolutionary Conservation == |
| + | [[Image:Consurf_key_small.gif|200px|right]] |
| + | Check<jmol> |
| + | <jmolCheckbox> |
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qn/1qnq_consurf.spt"</scriptWhenChecked> |
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| + | <text>to colour the structure by Evolutionary Conservation</text> |
| + | </jmolCheckbox> |
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1qnq ConSurf]. |
| + | <div style="clear:both"></div> |
| | | |
- | '''THE 3-D STRUCTURE OF A TRICHODERMA REESEI B-MANNANASE FROM GLYCOSIDE HYDROLASE FAMILY 5'''
| + | ==See Also== |
- | | + | *[[Mannosidase 3D structures|Mannosidase 3D structures]] |
- | | + | == References == |
- | ==Overview== | + | <references/> |
- | 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.
| + | __TOC__ |
- | | + | </StructureSection> |
- | ==About this Structure==
| + | [[Category: Large Structures]] |
- | 1QNQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Hypocrea_jecorina Hypocrea jecorina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QNQ OCA].
| + | |
- | | + | |
- | ==Reference== | + | |
- | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10666621 10666621]
| + | |
- | [[Category: Hypocrea jecorina]]
| + | |
- | [[Category: Mannan endo-1,4-beta-mannosidase]]
| + | |
- | [[Category: Single protein]]
| + | |
- | [[Category: Murshudov, G.]]
| + | |
- | [[Category: Penttila, M.]]
| + | |
- | [[Category: Sabini, E.]]
| + | |
- | [[Category: Schubert, H.]]
| + | |
- | [[Category: Siika-Aho, M.]]
| + | |
- | [[Category: Wilson, K S.]]
| + | |
- | [[Category: Anomalous scattering]]
| + | |
- | [[Category: Mannanase]] | + | |
| [[Category: Trichoderma reesei]] | | [[Category: Trichoderma reesei]] |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:29:38 2008''
| + | [[Category: Murshudov G]] |
| + | [[Category: Penttila M]] |
| + | [[Category: Sabini E]] |
| + | [[Category: Schubert H]] |
| + | [[Category: Siika-Aho M]] |
| + | [[Category: Wilson KS]] |
| Structural highlights
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, Ref.3, Ref.4, PubMed:8529653). Also has transglycosylation activity. Transglycosylation of two mannotrioses into a mannohexaose is the major transglycosylation route (PubMed:8529653, Ref.7, PubMed:24950755).[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.
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
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