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5kzd

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==N-acetylneuraminate lyase from methicillin-resistant Staphylococcus aureus with bound sialic acid alditol==
==N-acetylneuraminate lyase from methicillin-resistant Staphylococcus aureus with bound sialic acid alditol==
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<StructureSection load='5kzd' size='340' side='right' caption='[[5kzd]], [[Resolution|resolution]] 2.33&Aring;' scene=''>
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<StructureSection load='5kzd' size='340' side='right'caption='[[5kzd]], [[Resolution|resolution]] 2.33&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5kzd]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KZD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KZD FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5kzd]] is a 4 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=5KZD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KZD FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=RCJ:(2~{S},4~{S},5~{R},6~{R},7~{S},8~{R})-5-ACETAMIDO-2,4,6,7,8,9-HEXAKIS(OXIDANYL)NONANOIC+ACID'>RCJ</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.334&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5kze|5kze]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=RCJ:(2~{S},4~{S},5~{R},6~{R},7~{S},8~{R})-5-ACETAMIDO-2,4,6,7,8,9-HEXAKIS(OXIDANYL)NONANOIC+ACID'>RCJ</scene></td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5kzd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kzd OCA], [https://pdbe.org/5kzd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kzd RCSB], [https://www.ebi.ac.uk/pdbsum/5kzd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kzd ProSAT]</span></td></tr>
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<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=5kzd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kzd OCA], [http://pdbe.org/5kzd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kzd RCSB], [http://www.ebi.ac.uk/pdbsum/5kzd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kzd ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/NANA_STAA3 NANA_STAA3]] Catalyzes the reversible aldol cleavage of N-acetylneuraminic acid (sialic acid; Neu5Ac) to form pyruvate and N-acetylmannosamine (ManNAc) via a Schiff base intermediate.
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[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).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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==See Also==
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*[[N-acetylneuraminate lyase 3D structures|N-acetylneuraminate lyase 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5kzd" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: N-acetylneuraminate lyase]]
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[[Category: Large Structures]]
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[[Category: Dobson, R C.J]]
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[[Category: Staphylococcus aureus subsp. aureus USA300]]
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[[Category: Fairbanks, A J]]
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[[Category: Dobson RCJ]]
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[[Category: Friemann, R]]
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[[Category: Fairbanks AJ]]
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[[Category: Muscroft-Taylor, A C]]
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[[Category: Friemann R]]
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[[Category: North, R A]]
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[[Category: Muscroft-Taylor AC]]
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[[Category: Pearce, F G]]
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[[Category: North RA]]
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[[Category: Watson, A J.A]]
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[[Category: Pearce FG]]
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[[Category: Inhibitor]]
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[[Category: Watson AJA]]
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[[Category: Lyase]]
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[[Category: Tim-barrel]]
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Current revision

N-acetylneuraminate lyase from methicillin-resistant Staphylococcus aureus with bound sialic acid alditol

PDB ID 5kzd

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