4ak6: Difference between revisions
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==BpGH117_H302E mutant glycoside hydrolase== | ==BpGH117_H302E mutant glycoside hydrolase== | ||
<StructureSection load='4ak6' size='340' side='right' caption='[[4ak6]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='4ak6' size='340' side='right'caption='[[4ak6]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ak6]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4ak6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Phocaeicola_plebeius Phocaeicola plebeius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AK6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AK6 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ak6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ak6 OCA], [https://pdbe.org/4ak6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ak6 RCSB], [https://www.ebi.ac.uk/pdbsum/4ak6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ak6 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/B5CY74_PHOPM B5CY74_PHOPM] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[Galactosidase|Galactosidase]] | *[[Galactosidase 3D structures|Galactosidase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Boraston | [[Category: Phocaeicola plebeius]] | ||
[[Category: Hehemann | [[Category: Boraston AB]] | ||
[[Category: Smyth | [[Category: Hehemann JH]] | ||
[[Category: Vocadlo | [[Category: Smyth L]] | ||
[[Category: Yadav | [[Category: Vocadlo DJ]] | ||
[[Category: Yadav A]] | |||
Latest revision as of 13:51, 9 May 2024
BpGH117_H302E mutant glycoside hydrolaseBpGH117_H302E mutant glycoside hydrolase
Structural highlights
FunctionPublication Abstract from PubMedAgars are abundant polysaccharides from marine red algae and their chemical structure consists of alternating D- galactose and 3,6-anhydro-L-galactose residues, the latter of which is presumed to make the polymer recalcitrant to degradation by most terrestrial bacteria. Here we study a family 117 glycoside hydrolase (BpGH117) encoded within a recently discovered locus from the human gut bacterium Bacteroides plebeius. Consistent with this locus being involved in agarocolloid degradation, we show BpGH117 is an exo-acting 3,6-anhydro-alpha-(1,3)-L-galactosidase that removes the 3,6-anhydro-galactose from the non-reducing end of neoagaro-oligosaccharides. A Michaelis-complex of BpGH117 with neoagarobiose reveals the distortion of the constrained 3,6-anhydro-L-galactose into a conformation that favours catalysis. Furthermore, this complex, supported by analysis of site-directed mutants, provides evidence for and organization of the active site and positioning of the catalytic residues that is consistent with an inverting mechanism of catalysis and suggests that a histidine residue acts as the general acid. This latter feature differs from the vast majority of glycoside hydrolases, which use a carboxylic acid, highlighting the alternative strategies that enzymes may employ in catalyzing the cleavage of glycosidic bonds. Analysis of a keystone enzyme in agar hydrolysis provides insight into polysaccharide degradation from red seaweeds.,Hehemann JH, Smyth L, Yadav A, Vocadlo DJ, Boraston AB J Biol Chem. 2012 Mar 5. PMID:22393053[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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