View source for 5kze


==N-acetylneuraminate lyase from methicillin-resistant Staphylococcus aureus==
<StructureSection load='5kze' size='340' side='right'caption='[[5kze]], [[Resolution|resolution]] 1.74&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5kze]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_USA300 Staphylococcus aureus subsp. aureus USA300]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KZE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KZE 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]] 1.74&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5kze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kze OCA], [https://pdbe.org/5kze PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kze RCSB], [https://www.ebi.ac.uk/pdbsum/5kze PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kze ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NANA_STAA8 NANA_STAA8] Catalyzes the cleavage of N-acetylneuraminic acid (sialic acid) to form pyruvate and N-acetylmannosamine via a Schiff base intermediate (By similarity).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
N-Acetylneuraminate lyase is the first committed enzyme in the degradation of sialic acid by bacterial pathogens. In this study, we analyzed the kinetic parameters of N-acetylneuraminate lyase from methicillin-resistant Staphylococcus aureus (MRSA). We determined that the enzyme has a relatively high KM of 3.2 mm, suggesting that flux through the catabolic pathway is likely to be controlled by this enzyme. Our data indicate that sialic acid alditol, a known inhibitor of N-acetylneuraminate lyase enzymes, is a stronger inhibitor of MRSA N-acetylneuraminate lyase than of Clostridium perfringens N-acetylneuraminate lyase. Our analysis of the crystal structure of ligand-free and 2R-sialic acid alditol-bound MRSA N-acetylneuraminate lyase suggests that subtle dynamic differences in solution and/or altered binding interactions within the active site may account for species-specific inhibition.

Structure and inhibition of N-acetylneuraminate lyase from methicillin-resistant Staphylococcus aureus.,North RA, Watson AJ, Pearce FG, Muscroft-Taylor AC, Friemann R, Fairbanks AJ, Dobson RC FEBS Lett. 2016 Dec;590(23):4414-4428. doi: 10.1002/1873-3468.12462. Epub 2016, Nov 7. PMID:27943302<ref>PMID:27943302</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5kze" style="background-color:#fffaf0;"></div>

==See Also==
*[[N-acetylneuraminate lyase 3D structures|N-acetylneuraminate lyase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Staphylococcus aureus subsp. aureus USA300]]
[[Category: Dobson RCJ]]
[[Category: Fairbanks AJ]]
[[Category: Friemann R]]
[[Category: Muscroft-Taylor AC]]
[[Category: North RA]]
[[Category: Pearce FG]]
[[Category: Watson AJA]]