5y6t
From Proteopedia
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==Crystal structure of endo-1,4-beta-mannanase from Eisenia fetida== | ==Crystal structure of endo-1,4-beta-mannanase from Eisenia fetida== | ||
| - | <StructureSection load='5y6t' size='340' side='right' caption='[[5y6t]], [[Resolution|resolution]] 1.70Å' scene=''> | + | <StructureSection load='5y6t' size='340' side='right'caption='[[5y6t]], [[Resolution|resolution]] 1.70Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5y6t]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y6T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Y6T FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5y6t]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Eisfe Eisfe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y6T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Y6T FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></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=5y6t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y6t OCA], [http://pdbe.org/5y6t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5y6t RCSB], [http://www.ebi.ac.uk/pdbsum/5y6t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5y6t 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=5y6t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y6t OCA], [http://pdbe.org/5y6t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5y6t RCSB], [http://www.ebi.ac.uk/pdbsum/5y6t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5y6t ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The endo-1,4-beta-mannanases (Ef-Man) gene from Eisenia fetida was determined to consist of 1131bp and encode a 377 amino acid protein. The amino acid sequence showed similarity with the endo-1,4-beta-mannanases of Daphnia pulex (62%), Cryptopygus antarcticus (64%), Crassostrea gigas (61%), Mytilus edulis (60%), and Aplysia kurodai (58%). The gene encoding mature Ef-Man was expressed in Pichia pastoris (GS115 strain). Based on SDS-PAGE analysis, the molecular mass of the purified recombinant Ef-Man (rEf-Man) was estimated to be 39kDa. All catalytically important residues of endo-1,4-beta-mannanases in the glycoside hydrolase (GH) family 5 were conserved in Ef-Man. The optimal temperature for rEf-Man was identified as 60 degrees C. HPLC and HPAEC analyses suggest that Ef-Man requires at least six subsites for efficient hydrolysis and is capable of performing transglycosylation reactions. The overall structure of rEf-Man is similar to those of GH5 family proteins, and tertiary structures around the active site are conserved among endo-1,4-beta-mannanase families. X-ray crystallographic analysis supports the hydrolysis and transglycosylation reaction mechanism determined by HPLC and HPAEC analyses. | ||
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| + | Gene cloning, expression, and X-ray crystallographic analysis of a beta-mannanase from Eisenia fetida.,Ueda M, Hirano Y, Fukuhara H, Naka Y, Nakazawa M, Sakamoto T, Ogata Y, Tamada T Enzyme Microb Technol. 2018 Oct;117:15-22. doi: 10.1016/j.enzmictec.2018.05.014. , Epub 2018 May 25. PMID:30037547<ref>PMID:30037547</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5y6t" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Eisfe]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Hirano, Y]] | [[Category: Hirano, Y]] | ||
[[Category: Tamada, T]] | [[Category: Tamada, T]] | ||
Revision as of 12:42, 25 December 2019
Crystal structure of endo-1,4-beta-mannanase from Eisenia fetida
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