|
|
| Line 3: |
Line 3: |
| | <StructureSection load='5kze' size='340' side='right'caption='[[5kze]], [[Resolution|resolution]] 1.74Å' scene=''> | | <StructureSection load='5kze' size='340' side='right'caption='[[5kze]], [[Resolution|resolution]] 1.74Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5kze]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Staa3 Staa3]. 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 [http://proteopedia.org/fgij/fg.htm?mol=5KZE FirstGlance]. <br> | + | <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='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> | + | </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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5kzd|5kzd]]</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nanA, SAUSA300_0315 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=367830 STAA3])</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> |
| - | <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://proteopedia.org/fgij/fg.htm?mol=5kze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kze OCA], [http://pdbe.org/5kze PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kze RCSB], [http://www.ebi.ac.uk/pdbsum/5kze PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kze ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == 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. | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 21: |
Line 19: |
| | </div> | | </div> |
| | <div class="pdbe-citations 5kze" style="background-color:#fffaf0;"></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 == |
| | <references/> | | <references/> |
| Line 26: |
Line 27: |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: N-acetylneuraminate lyase]] | + | [[Category: Staphylococcus aureus subsp. aureus USA300]] |
| - | [[Category: Staa3]]
| + | [[Category: Dobson RCJ]] |
| - | [[Category: Dobson, R C.J]] | + | [[Category: Fairbanks AJ]] |
| - | [[Category: Fairbanks, A J]] | + | [[Category: Friemann R]] |
| - | [[Category: Friemann, R]] | + | [[Category: Muscroft-Taylor AC]] |
| - | [[Category: Muscroft-Taylor, A C]] | + | [[Category: North RA]] |
| - | [[Category: North, R A]] | + | [[Category: Pearce FG]] |
| - | [[Category: Pearce, F G]] | + | [[Category: Watson AJA]] |
| - | [[Category: Watson, A J.A]] | + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Tim-barrel]]
| + | |
| Structural highlights
Function
NANA_STAA8 Catalyzes the cleavage of N-acetylneuraminic acid (sialic acid) to form pyruvate and N-acetylmannosamine via a Schiff base intermediate (By similarity).
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ North RA, Watson AJ, Pearce FG, Muscroft-Taylor AC, Friemann R, Fairbanks AJ, Dobson RC. Structure and inhibition of N-acetylneuraminate lyase from methicillin-resistant Staphylococcus aureus. FEBS Lett. 2016 Dec;590(23):4414-4428. doi: 10.1002/1873-3468.12462. Epub 2016, Nov 7. PMID:27943302 doi:http://dx.doi.org/10.1002/1873-3468.12462
|
