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| | ==Crystal structure of beta-1,4-D-mannanase from Cryptopygus antarcticus== | | ==Crystal structure of beta-1,4-D-mannanase from Cryptopygus antarcticus== |
| - | <StructureSection load='4oou' size='340' side='right' caption='[[4oou]], [[Resolution|resolution]] 2.36Å' scene=''> | + | <StructureSection load='4oou' size='340' side='right'caption='[[4oou]], [[Resolution|resolution]] 2.36Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4oou]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OOU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OOU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4oou]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cryptopygus_antarcticus Cryptopygus antarcticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OOU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OOU FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.36Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ooz|4ooz]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4oou FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oou OCA], [https://pdbe.org/4oou PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4oou RCSB], [https://www.ebi.ac.uk/pdbsum/4oou PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4oou ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4oou FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oou OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4oou RCSB], [http://www.ebi.ac.uk/pdbsum/4oou PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/MANA_CRYAT MANA_CRYAT] Hydrolyzes 1,4-beta linked polysaccharide backbones of mannans. Has high activity toward locust bean gum (PubMed:18579426, PubMed:25082572). Also active toward konjac and beta-1,4-mannan. Hydrolyzes mannotetraose (M4) and mannopentaose (M5) to mannobiose (M2) and mannotriose (M3) with a little production of mannose (M1). Hydrolyzes beta-1,4-mannan to M2, M3 and M4. Hardly hydrolyzes M2 and M3. Does not hydrolyze p-nitrophenyl-beta-D-mannopyranoside, gua-gum, carboxymethyl cellulose, soluble starch or laminarin (PubMed:18579426).<ref>PMID:18579426</ref> <ref>PMID:25082572</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 4oou" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Mannan endo-1,4-beta-mannosidase]] | + | [[Category: Cryptopygus antarcticus]] |
| - | [[Category: An, Y J.]] | + | [[Category: Large Structures]] |
| - | [[Category: Cha, S S.]] | + | [[Category: An YJ]] |
| - | [[Category: Jeong, C S.]] | + | [[Category: Cha S-S]] |
| - | [[Category: Kim, M K.]] | + | [[Category: Jeong C-S]] |
| - | [[Category: Hydrolase]]
| + | [[Category: Kim M-K]] |
| - | [[Category: Tim barrel]]
| + | |
| Structural highlights
Function
MANA_CRYAT Hydrolyzes 1,4-beta linked polysaccharide backbones of mannans. Has high activity toward locust bean gum (PubMed:18579426, PubMed:25082572). Also active toward konjac and beta-1,4-mannan. Hydrolyzes mannotetraose (M4) and mannopentaose (M5) to mannobiose (M2) and mannotriose (M3) with a little production of mannose (M1). Hydrolyzes beta-1,4-mannan to M2, M3 and M4. Hardly hydrolyzes M2 and M3. Does not hydrolyze p-nitrophenyl-beta-D-mannopyranoside, gua-gum, carboxymethyl cellulose, soluble starch or laminarin (PubMed:18579426).[1] [2]
Publication Abstract from PubMed
Endo-beta-1,4-d-mannanase from the Antarctic springtail, Cryptopygus antarcticus (CaMan), is a cold-adapted beta-mannanase that has the lowest optimum temperature (30 degrees C) of all known beta-mannanases. Here, we report the apo- and mannopentaose (M5) complex structures of CaMan. Structural comparison of CaMan with other beta-mannanases from the multicellular animals reveals that CaMan has an extended loop that alters topography of the active site. Structural and mutational analyses suggest that this extended loop is linked to the cold-adapted enzymatic activity. From the CaMan-M5 complex structure, we defined the mannose-recognition subsites and observed unreported M5 binding site on the surface of CaMan. Proteins 2014; 82:3217-3223. (c) 2014 Wiley Periodicals, Inc.
Structure-based investigation into the functional roles of the extended loop and substrate-recognition sites in an endo-beta-1,4-d-mannanase from the Antarctic springtail, Cryptopygus antarcticus.,Kim MK, An YJ, Song JM, Jeong CS, Kang MH, Kwon KK, Lee YH, Cha SS Proteins. 2014 Nov;82(11):3217-23. doi: 10.1002/prot.24655. Epub 2014 Aug 19. PMID:25082572[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Song JM, Nam KW, Kang SG, Kim CG, Kwon ST, Lee YH. Molecular cloning and characterization of a novel cold-active beta-1,4-D-mannanase from the Antarctic springtail, Cryptopygus antarcticus. Comp Biochem Physiol B Biochem Mol Biol. 2008 Sep;151(1):32-40. doi: , 10.1016/j.cbpb.2008.05.005. Epub 2008 May 18. PMID:18579426 doi:http://dx.doi.org/10.1016/j.cbpb.2008.05.005
- ↑ Kim MK, An YJ, Song JM, Jeong CS, Kang MH, Kwon KK, Lee YH, Cha SS. Structure-based investigation into the functional roles of the extended loop and substrate-recognition sites in an endo-beta-1,4-d-mannanase from the Antarctic springtail, Cryptopygus antarcticus. Proteins. 2014 Nov;82(11):3217-23. doi: 10.1002/prot.24655. Epub 2014 Aug 19. PMID:25082572 doi:http://dx.doi.org/10.1002/prot.24655
- ↑ Kim MK, An YJ, Song JM, Jeong CS, Kang MH, Kwon KK, Lee YH, Cha SS. Structure-based investigation into the functional roles of the extended loop and substrate-recognition sites in an endo-beta-1,4-d-mannanase from the Antarctic springtail, Cryptopygus antarcticus. Proteins. 2014 Nov;82(11):3217-23. doi: 10.1002/prot.24655. Epub 2014 Aug 19. PMID:25082572 doi:http://dx.doi.org/10.1002/prot.24655
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