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| | <StructureSection load='6k35' size='340' side='right'caption='[[6k35]], [[Resolution|resolution]] 2.36Å' scene=''> | | <StructureSection load='6k35' size='340' side='right'caption='[[6k35]], [[Resolution|resolution]] 2.36Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6k35]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"achromobacter_harveyi"_johnson_and_shunk_1936 "achromobacter harveyi" johnson and shunk 1936]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K35 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6K35 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6k35]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_harveyi Vibrio harveyi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K35 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6K35 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NGT:3AR,5R,6S,7R,7AR-5-HYDROXYMETHYL-2-METHYL-5,6,7,7A-TETRAHYDRO-3AH-PYRANO[3,2-D]THIAZOLE-6,7-DIOL'>NGT</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]] 2.36Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[6ezr|6ezr]], [[6ezs|6ezs]], [[6ezt|6ezt]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NGT:3AR,5R,6S,7R,7AR-5-HYDROXYMETHYL-2-METHYL-5,6,7,7A-TETRAHYDRO-3AH-PYRANO[3,2-D]THIAZOLE-6,7-DIOL'>NGT</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-N-acetylhexosaminidase Beta-N-acetylhexosaminidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.52 3.2.1.52] </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=6k35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k35 OCA], [https://pdbe.org/6k35 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6k35 RCSB], [https://www.ebi.ac.uk/pdbsum/6k35 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6k35 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6k35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k35 OCA], [http://pdbe.org/6k35 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6k35 RCSB], [http://www.ebi.ac.uk/pdbsum/6k35 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6k35 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/D9ISE0_VIBHA D9ISE0_VIBHA] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6k35" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6k35" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Beta-N-acetylhexosaminidase 3D structures|Beta-N-acetylhexosaminidase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Achromobacter harveyi johnson and shunk 1936]] | |
| - | [[Category: Beta-N-acetylhexosaminidase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Berg, B van den]] | + | [[Category: Vibrio harveyi]] |
| - | [[Category: Bulmer, D M]] | + | [[Category: Bulmer DM]] |
| - | [[Category: Meekrathok, P]] | + | [[Category: Meekrathok P]] |
| - | [[Category: Stubbs, K A]] | + | [[Category: Stubbs KA]] |
| - | [[Category: Suginta, W]] | + | [[Category: Suginta W]] |
| - | [[Category: Anti-bacterial agent]] | + | [[Category: Van den Berg B]] |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
D9ISE0_VIBHA
Publication Abstract from PubMed
Vibrio spp. play a vital role in the recycling of chitin in oceans, but several Vibrio strains are highly infectious to aquatic animals and humans. These bacteria require chitin for growth; thus, potent inhibitors of chitin-degrading enzymes could serve as candidate drugs against Vibrio infections. This study examined NAG-thiazoline (NGT)-mediated inhibition of a recombinantly expressed GH20 beta-N-acetylglucosaminidase, namely VhGlcNAcase from Vibrio campbellii (formerly V. harveyi) ATCC BAA-1116. NGT strongly inhibited VhGlcNAcase with an IC50 of 11.9 +/- 1.0 mum and Ki 62 +/- 3 microm, respectively. NGT was also found to completely inhibit the growth of V. campbellii strain 650 with an minimal inhibitory concentration value of 0.5 microm. ITC data analysis showed direct binding of NGT to VhGlcNAcase with a Kd of 32 +/- 1.2 mum. The observed DeltaG degrees binding of -7.56 kcal.mol(-1) is the result of a large negative enthalpy change and a small positive entropic compensation, suggesting that NGT binding is enthalpy-driven. The structural complex shows that NGT fully occupies the substrate-binding pocket of VhGlcNAcase and makes an exclusive hydrogen bond network, as well as hydrophobic interactions with the conserved residues around the -1 subsite. Our results strongly suggest that NGT could serve as an excellent scaffold for further development of antimicrobial agents against Vibrio infections. DATABASE: Structural data are available in PDB database under the accession number 6K35.
NAG-thiazoline is a potent inhibitor of the Vibrio campbellii GH20 beta-N-Acetylglucosaminidase.,Meekrathok P, Stubbs KA, Aunkham A, Kaewmaneewat A, Kardkuntod A, Bulmer DM, van den Berg B, Suginta W FEBS J. 2020 Mar 7. doi: 10.1111/febs.15283. PMID:32145141[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Meekrathok P, Stubbs KA, Aunkham A, Kaewmaneewat A, Kardkuntod A, Bulmer DM, van den Berg B, Suginta W. NAG-thiazoline is a potent inhibitor of the Vibrio campbellii GH20 beta-N-Acetylglucosaminidase. FEBS J. 2020 Mar 7. doi: 10.1111/febs.15283. PMID:32145141 doi:http://dx.doi.org/10.1111/febs.15283
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