6moy

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (14:44, 13 March 2024) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='6moy' size='340' side='right'caption='[[6moy]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='6moy' size='340' side='right'caption='[[6moy]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[6moy]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bifld Bifld]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MOY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MOY FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[6moy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bifidobacterium_longum_DJO10A Bifidobacterium longum DJO10A]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MOY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MOY FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 2.5&#8491;</td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BLD_0195 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=205913 BIFLD])</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></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=6moy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6moy OCA], [http://pdbe.org/6moy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6moy RCSB], [http://www.ebi.ac.uk/pdbsum/6moy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6moy ProSAT]</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=6moy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6moy OCA], [https://pdbe.org/6moy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6moy RCSB], [https://www.ebi.ac.uk/pdbsum/6moy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6moy ProSAT]</span></td></tr>
</table>
</table>
-
<div style="background-color:#fffaf0;">
+
== Function ==
-
== Publication Abstract from PubMed ==
+
[https://www.uniprot.org/uniprot/B3DQP5_BIFLD B3DQP5_BIFLD]
-
Bifidobacteria represent one of the first colonizers of human gut microbiota, providing to this ecosystem better health and nutrition. To maintain a mutualistic relationship, they have enzymes to degrade and use complex carbohydrates non-digestible by their hosts. To succeed in the densely populated gut environment, they evolved molecular strategies that remain poorly understood. Herein, we report a novel mechanism found in probiotic Bifidobacteria for the depolymerization of the ubiquitous 2-acetamido-2-deoxy-4-O-(beta-d-mannopyranosyl)-d-glucopyranose (Man-beta-1,4-GlcNAc), a disaccharide that composes the universal core of eukaryotic N-glycans. In contrast to Bacteroidetes, these Bifidobacteria have a specialist and strain-specific beta-mannosidase that contains three distinctive structural elements conferring high selectivity for Man-beta-1,4-GlcNAc: a lid that undergoes conformational changes upon substrate binding, a tryptophan residue swapped between the two dimeric subunits to accommodate the GlcNAc moiety, and a Rossmann fold subdomain strategically located near to the active site pocket. These key structural elements for Man-beta-1,4-GlcNAc specificity are highly conserved in Bifidobacterium species adapted to the gut of a wide range of social animals, including bee, pig, rabbit, and human. Together, our findings uncover an unprecedented molecular strategy employed by Bifidobacteria to selectively uptake carbohydrates from N-glycans in social hosts.
+
-
N-glycan Utilization by Bifidobacterium Gut Symbionts Involves a Specialist beta-Mannosidase.,Cordeiro RL, Pirolla RAS, Persinoti GF, Gozzo FC, de Giuseppe PO, Murakami MT J Mol Biol. 2019 Jan 11. pii: S0022-2836(19)30006-3. doi:, 10.1016/j.jmb.2018.12.017. PMID:30641082<ref>PMID:30641082</ref>
+
==See Also==
-
 
+
*[[Mannosidase 3D structures|Mannosidase 3D structures]]
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 6moy" style="background-color:#fffaf0;"></div>
+
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Bifld]]
+
[[Category: Bifidobacterium longum DJO10A]]
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Giuseppe, P O]]
+
[[Category: Giuseppe PO]]
-
[[Category: Lorizolla-Cordeiro, R]]
+
[[Category: Lorizolla-Cordeiro R]]
-
[[Category: Murakami, M T]]
+
[[Category: Murakami MT]]
-
[[Category: Beta-mannosidase]]
+
-
[[Category: Family gh5]]
+
-
[[Category: Hydrolase]]
+
-
[[Category: Subfamily 18]]
+

Current revision

Crystal structure of the E257A mutant of BlMan5B in complex with GlcNAc (co-crystallization)

PDB ID 6moy

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools