5kzd
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==N-acetylneuraminate lyase from methicillin-resistant Staphylococcus aureus with bound sialic acid alditol== | |
| + | <StructureSection load='5kzd' size='340' side='right' caption='[[5kzd]], [[Resolution|resolution]] 2.33Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <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> | ||
| + | </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> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5kze|5kze]]</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=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> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[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. | ||
| + | <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> |
| + | <div class="pdbe-citations 5kzd" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: N-acetylneuraminate lyase]] | ||
| + | [[Category: Dobson, R C.J]] | ||
| + | [[Category: Fairbanks, A J]] | ||
| + | [[Category: Friemann, R]] | ||
| + | [[Category: Muscroft-Taylor, A C]] | ||
| + | [[Category: North, R A]] | ||
| + | [[Category: Pearce, F G]] | ||
| + | [[Category: Watson, A J.A]] | ||
| + | [[Category: Inhibitor]] | ||
| + | [[Category: Lyase]] | ||
| + | [[Category: Tim-barrel]] | ||
Revision as of 16:30, 18 January 2017
N-acetylneuraminate lyase from methicillin-resistant Staphylococcus aureus with bound sialic acid alditol
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