View source for 5zka


==Crystal structure of N-acetylneuraminate lyase from Fusobacterium nucleatum complexed with Pyruvate==
<StructureSection load='5zka' size='340' side='right'caption='[[5zka]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5zka]] is a 2 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=5ZKA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZKA 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]] 1.76&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=KPI:(2S)-2-AMINO-6-[(1-HYDROXY-1-OXO-PROPAN-2-YLIDENE)AMINO]HEXANOIC+ACID'>KPI</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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=5zka FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zka OCA], [https://pdbe.org/5zka PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zka RCSB], [https://www.ebi.ac.uk/pdbsum/5zka PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zka ProSAT]</span></td></tr>
</table>
== Function ==
[https://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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5zka" style="background-color:#fffaf0;"></div>

==See Also==
*[[N-acetylneuraminate lyase|N-acetylneuraminate lyase]]
*[[N-acetylneuraminate lyase 3D structures|N-acetylneuraminate lyase 3D structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Fusobacterium nucleatum subsp. nucleatum ATCC 25586]]
[[Category: Large Structures]]
[[Category: Kumar JP]]
[[Category: Nayak V]]
[[Category: Ramaswamy S]]
[[Category: Rao H]]