5y6t: Difference between revisions
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New page: '''Unreleased structure''' The entry 5y6t is ON HOLD Authors: Hirano, Y., Ueda, M., Tamada, T. Description: Crystal structure of endo-1,4-beta-mannanase from Eisenia fetida [[Category:... |
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The | ==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=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5y6t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Eisenia_fetida Eisenia fetida]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5Y6T FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=5y6t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y6t OCA], [https://pdbe.org/5y6t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5y6t RCSB], [https://www.ebi.ac.uk/pdbsum/5y6t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5y6t ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A3B6UEQ6_EISFE A0A3B6UEQ6_EISFE] | |||
<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. | |||
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> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5y6t" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Eisenia fetida]] | |||
[[Category: Large Structures]] | |||
[[Category: Hirano Y]] | |||
[[Category: Tamada T]] | |||
[[Category: Ueda M]] | |||
Latest revision as of 08:23, 22 November 2023
Crystal structure of endo-1,4-beta-mannanase from Eisenia fetida
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