7ebp: Difference between revisions
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The | ==The structural analysis of A.Muciniphila sulfatase== | ||
<StructureSection load='7ebp' size='340' side='right'caption='[[7ebp]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7ebp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Akkermansia_muciniphila_ATCC_BAA-835 Akkermansia muciniphila ATCC BAA-835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7EBP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7EBP 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]] 1.8000005Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=7ebp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ebp OCA], [https://pdbe.org/7ebp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ebp RCSB], [https://www.ebi.ac.uk/pdbsum/7ebp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ebp ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/B2UR15_AKKM8 B2UR15_AKKM8] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Akkermansia muciniphila, an anaerobic Gram-negative bacterium, is a major intestinal commensal bacterium that can modulate the host immune response. It colonizes the mucosal layer and produces nutrients for the gut mucosa and other commensal bacteria. It is believed that mucin desulfation is the rate-limiting step in the mucin-degradation process, and bacterial sulfatases that carry out mucin desulfation have been well studied. However, little is known about the structural characteristics of A. muciniphila sulfatases. Here, the crystal structure of the premature form of the A. muciniphila sulfatase AmAS was determined. Structural analysis combined with docking experiments defined the critical active-site residues that are responsible for catalysis. The loop regions I-V were proposed to be essential for substrate binding. Structure-based sequence alignment and structural superposition allow further elucidation of how different subclasses of formylglycine-dependent sulfatases (FGly sulfatases) adopt the same catalytic mechanism but exhibit diverse substrate specificities. These results advance the understanding of the substrate-recognition mechanisms of A. muciniphila FGly-type sulfatases. Structural variations around the active sites account for the different substrate-binding properties. These results will enhance the understanding of the roles of bacterial sulfatases in the metabolism of glycans and host-microbe interactions in the human gut environment. | |||
Structural analysis of the sulfatase AmAS from Akkermansia muciniphila.,Li CC, Tang XY, Zhu YB, Song YJ, Zhao NL, Huang Q, Mou XY, Luo GH, Liu TG, Tong AP, Tang H, Bao R Acta Crystallogr D Struct Biol. 2021 Dec 1;77(Pt 12):1614-1623. doi:, 10.1107/S2059798321010317. Epub 2021 Nov 29. PMID:34866616<ref>PMID:34866616</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7ebp" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Sulfatase 3D structures|Sulfatase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Akkermansia muciniphila ATCC BAA-835]] | |||
[[Category: Large Structures]] | |||
[[Category: Bao R]] | |||
[[Category: Huang Q]] | |||
[[Category: Li CC]] | |||
[[Category: Liu TG]] | |||
[[Category: Luo GH]] | |||
[[Category: Mou XY]] | |||
[[Category: Song YJ]] | |||
[[Category: Tang XY]] | |||
[[Category: Zhao NL]] | |||
[[Category: Zhu YB]] | |||
Latest revision as of 19:50, 29 November 2023
The structural analysis of A.Muciniphila sulfataseThe structural analysis of A.Muciniphila sulfatase
Structural highlights
FunctionPublication Abstract from PubMedAkkermansia muciniphila, an anaerobic Gram-negative bacterium, is a major intestinal commensal bacterium that can modulate the host immune response. It colonizes the mucosal layer and produces nutrients for the gut mucosa and other commensal bacteria. It is believed that mucin desulfation is the rate-limiting step in the mucin-degradation process, and bacterial sulfatases that carry out mucin desulfation have been well studied. However, little is known about the structural characteristics of A. muciniphila sulfatases. Here, the crystal structure of the premature form of the A. muciniphila sulfatase AmAS was determined. Structural analysis combined with docking experiments defined the critical active-site residues that are responsible for catalysis. The loop regions I-V were proposed to be essential for substrate binding. Structure-based sequence alignment and structural superposition allow further elucidation of how different subclasses of formylglycine-dependent sulfatases (FGly sulfatases) adopt the same catalytic mechanism but exhibit diverse substrate specificities. These results advance the understanding of the substrate-recognition mechanisms of A. muciniphila FGly-type sulfatases. Structural variations around the active sites account for the different substrate-binding properties. These results will enhance the understanding of the roles of bacterial sulfatases in the metabolism of glycans and host-microbe interactions in the human gut environment. Structural analysis of the sulfatase AmAS from Akkermansia muciniphila.,Li CC, Tang XY, Zhu YB, Song YJ, Zhao NL, Huang Q, Mou XY, Luo GH, Liu TG, Tong AP, Tang H, Bao R Acta Crystallogr D Struct Biol. 2021 Dec 1;77(Pt 12):1614-1623. doi:, 10.1107/S2059798321010317. Epub 2021 Nov 29. PMID:34866616[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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