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| | <StructureSection load='5zkn' size='340' side='right'caption='[[5zkn]], [[Resolution|resolution]] 2.21Å' scene=''> | | <StructureSection load='5zkn' size='340' side='right'caption='[[5zkn]], [[Resolution|resolution]] 2.21Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5zkn]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZKN OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5ZKN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5zkn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Fusobacterium_nucleatum_subsp._nucleatum_ATCC_25586 Fusobacterium nucleatum subsp. nucleatum ATCC 25586]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZKN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZKN FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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]] 2.205Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/N-acylglucosamine-6-phosphate_2-epimerase N-acylglucosamine-6-phosphate 2-epimerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.3.9 5.1.3.9] </span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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=5zkn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zkn OCA], [http://pdbe.org/5zkn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zkn RCSB], [http://www.ebi.ac.uk/pdbsum/5zkn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zkn 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=5zkn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zkn OCA], [https://pdbe.org/5zkn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zkn RCSB], [https://www.ebi.ac.uk/pdbsum/5zkn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zkn ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/NANE_FUSNN NANE_FUSNN]] Converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N-acetylglucosamine-6-phosphate (GlcNAc-6-P). | + | [https://www.uniprot.org/uniprot/NANE_FUSNN NANE_FUSNN] Converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N-acetylglucosamine-6-phosphate (GlcNAc-6-P). |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | Sialic acids are nine-carbon sugars that are found abundantly on the cell surfaces of mammals as glycoprotein or glycolipid complexes. Several Gram-negative and Gram-positive bacteria have the ability to scavenge and catabolize sialic acids to use as a carbon source. This gives them an advantage in colonizing sialic acid-rich environments. The genes of the sialic acid catabolic pathway are generally present as the operon nanAKE. The third gene in the operon encodes the enzyme N-acetylmannosamine-6-phosphate 2-epimerase (NanE), which catalyzes the conversion of N-acetylmannosamine 6-phosphate to N-acetylglucosamine 6-phosphate, thus committing it to enter glycolysis. The NanE enzyme belongs to the isomerase class of enzymes possessing the triose phosphate isomerase (TIM) barrel fold. Here, comparative structural and functional characterizations of the NanE epimerases from two pathogenic Gram-negative bacteria, Fusobacterium nucleatum (Fn) and Vibrio cholerae (Vc), have been carried out. Structures of NanE from Vc (VcNanE) with and without ligand bound have been determined to 1.7 and 2.7 A resolution, respectively. The structure of NanE from Fn (FnNanE) has been determined to 2.2 A resolution. The enzymes show kinetic parameters that are consistent with those of Clostridium perfringens NanE. These studies allowed an evaluation of whether NanE may be a good drug target against these pathogenic bacteria.
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| - | | + | |
| - | Crystal structures and kinetic analyses of N-acetylmannosamine-6-phosphate 2-epimerases from Fusobacterium nucleatum and Vibrio cholerae.,Manjunath L, Guntupalli SR, Currie MJ, North RA, Dobson RCJ, Nayak V, Subramanian R Acta Crystallogr F Struct Biol Commun. 2018 Jul 1;74(Pt 7):431-440. doi:, 10.1107/S2053230X18008543. Epub 2018 Jun 28. PMID:29969107<ref>PMID:29969107</ref>
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| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 5zkn" style="background-color:#fffaf0;"></div>
| + | |
| - | == References ==
| + | |
| - | <references/>
| + | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Fusobacterium nucleatum subsp. nucleatum ATCC 25586]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: N-acylglucosamine-6-phosphate 2-epimerase]]
| + | [[Category: Manjunath L]] |
| - | [[Category: Manjunath, L]] | + | |
| - | [[Category: Isomerase]]
| + | |
| - | [[Category: Sialic acid catabolic pathway epimerase]]
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