5zka
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of N-acetylneuraminate lyase from Fusobacterium nucleatum complexed with Pyruvate== | |
| + | <StructureSection load='5zka' size='340' side='right' caption='[[5zka]], [[Resolution|resolution]] 1.76Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5zka]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZKA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZKA FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=KPI:(2S)-2-AMINO-6-[(1-HYDROXY-1-OXO-PROPAN-2-YLIDENE)AMINO]HEXANOIC+ACID'>KPI</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/N-acetylneuraminate_lyase N-acetylneuraminate lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.3.3 4.1.3.3] </span></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=5zka FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zka OCA], [http://pdbe.org/5zka PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zka RCSB], [http://www.ebi.ac.uk/pdbsum/5zka PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zka ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/NANA_FUSNN NANA_FUSNN]] Catalyzes the reversible aldol cleavage of N-acetylneuraminic acid (sialic acid; Neu5Ac) to form pyruvate and N-acetylmannosamine (ManNAc) via a Schiff base intermediate. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | N-Acetyl-D-neuraminic acid lyase (NanA) catalyzes the breakdown of sialic acid (Neu5Ac) to N-acetyl-D-mannosamine (ManNAc) and pyruvate. NanA plays a key role in Neu5Ac catabolism in many pathogenic and bacterial commensals where sialic acid is available as a carbon and nitrogen source. Several pathogens or commensals decorate their surfaces with sialic acids as a strategy to escape host innate immunity. Catabolism of sialic acid is key to a range of host-pathogen interactions. In this study, atomic resolution structures of NanA from Fusobacterium nucleatum (FnNanA) in ligand-free and ligand-bound forms are reported at 2.32 and 1.76 A resolution, respectively. F. nucleatum is a Gram-negative pathogen that causes gingival and periodontal diseases in human hosts. Like other bacterial N-acetylneuraminate lyases, FnNanA also shares the triosephosphate isomerase (TIM)-barrel fold. As observed in other homologous enzymes, FnNanA forms a tetramer. In order to characterize the structure-function relationship, the steady-state kinetic parameters of the enzyme are also reported. | ||
| - | + | Crystal structures and kinetics of N-acetylneuraminate lyase from Fusobacterium nucleatum.,Kumar JP, Rao H, Nayak V, Ramaswamy S Acta Crystallogr F Struct Biol Commun. 2018 Nov 1;74(Pt 11):725-732. doi:, 10.1107/S2053230X18012992. Epub 2018 Oct 17. PMID:30387778<ref>PMID:30387778</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5zka" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: N-acetylneuraminate lyase]] | ||
| + | [[Category: Kumar, J P]] | ||
| + | [[Category: Nayak, V]] | ||
| + | [[Category: Ramaswamy, S]] | ||
| + | [[Category: Rao, H]] | ||
| + | [[Category: Lyase]] | ||
| + | [[Category: Schiff base]] | ||
| + | [[Category: Sialic acid catabolism]] | ||
| + | [[Category: Tim-barrel]] | ||
Revision as of 06:31, 5 December 2018
Crystal structure of N-acetylneuraminate lyase from Fusobacterium nucleatum complexed with Pyruvate
| |||||||||||
