5kze: Difference between revisions
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New page: '''Unreleased structure''' The entry 5kze is ON HOLD Authors: North, R.A., Watson, A.J.A., Pearce, F.G., Muscroft-Taylor, A.C., Friemann, R., Fairbanks, A.J., Dobson, R.C.J. Descriptio... |
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==N-acetylneuraminate lyase from methicillin-resistant Staphylococcus aureus== | |||
<StructureSection load='5kze' size='340' side='right'caption='[[5kze]], [[Resolution|resolution]] 1.74Å' 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]] 1.74Å</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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5kze" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: | ==See Also== | ||
[[Category: | *[[N-acetylneuraminate lyase 3D structures|N-acetylneuraminate lyase 3D structures]] | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: Pearce | __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]] | |||
Latest revision as of 12:45, 4 October 2023
N-acetylneuraminate lyase from methicillin-resistant Staphylococcus aureus
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