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| | <StructureSection load='2wkj' size='340' side='right'caption='[[2wkj]], [[Resolution|resolution]] 1.45Å' scene=''> | | <StructureSection load='2wkj' size='340' side='right'caption='[[2wkj]], [[Resolution|resolution]] 1.45Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2wkj]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WKJ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2WKJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2wkj]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WKJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WKJ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</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]] 1.45Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=KPI:(2S)-2-AMINO-6-[(1-HYDROXY-1-OXO-PROPAN-2-YLIDENE)AMINO]HEXANOIC+ACID'>KPI</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=KPI:(2S)-2-AMINO-6-[(1-HYDROXY-1-OXO-PROPAN-2-YLIDENE)AMINO]HEXANOIC+ACID'>KPI</scene>, <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1nal|1nal]], [[1hl2|1hl2]], [[1fdz|1fdz]], [[1fdy|1fdy]]</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=2wkj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wkj OCA], [https://pdbe.org/2wkj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wkj RCSB], [https://www.ebi.ac.uk/pdbsum/2wkj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wkj 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=2wkj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wkj OCA], [http://pdbe.org/2wkj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wkj RCSB], [http://www.ebi.ac.uk/pdbsum/2wkj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2wkj ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/NANA_ECOLI NANA_ECOLI] Catalyzes the cleavage of N-acetylneuraminic acid (sialic acid) to form pyruvate and N-acetylmannosamine via a Schiff base intermediate.[HAMAP-Rule:MF_01237] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Aldolase 3D structures|Aldolase 3D structures]] | + | *[[N-acetylneuraminate lyase 3D structures|N-acetylneuraminate lyase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: N-acetylneuraminate lyase]]
| + | [[Category: Berry A]] |
| - | [[Category: Berry, A]] | + | [[Category: Campeotto I]] |
| - | [[Category: Campeotto, I]] | + | [[Category: Carr SB]] |
| - | [[Category: Carr, S B]] | + | [[Category: Nelson AS]] |
| - | [[Category: Nelson, A S]] | + | [[Category: Pearson AR]] |
| - | [[Category: Pearson, A R]] | + | [[Category: Phillips SEV]] |
| - | [[Category: Phillips, S E.V]] | + | [[Category: Trinh CH]] |
| - | [[Category: Trinh, C H]] | + | |
| - | [[Category: Aldolase]]
| + | |
| - | [[Category: Carbohydrate metabolism]]
| + | |
| - | [[Category: Directed evolution]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: N-acetylneuraminic acid lyase]]
| + | |
| - | [[Category: Schiff base]]
| + | |
| - | [[Category: Sialic acid mimetic]]
| + | |
| Structural highlights
Function
NANA_ECOLI Catalyzes the cleavage of N-acetylneuraminic acid (sialic acid) to form pyruvate and N-acetylmannosamine via a Schiff base intermediate.[HAMAP-Rule:MF_01237]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The structure of a mutant variant of Escherichia coli N-acetyl-d-neuraminic acid lyase (NAL), E192N, in complex with pyruvate has been determined in a new crystal form. It crystallized in space group P2(1)2(1)2(1), with unit-cell parameters a = 78.3, b = 108.5, c = 148.3 angstrom. Pyruvate has been trapped in the active site as a Schiff base with the catalytic lysine (Lys165) without the need for reduction. Unlike the previously published crystallization conditions for the wild-type enzyme, in which a mother-liquor-derived sulfate ion is strongly bound in the catalytic pocket, the low-salt conditions described here will facilitate the determination of further E. coli NAL structures in complex with other activesite ligands.
Structure of an Escherichia coli N-acetyl-D-neuraminic acid lyase mutant, E192N, in complex with pyruvate at 1.45 angstrom resolution.,Campeotto I, Carr SB, Trinh CH, Nelson AS, Berry A, Phillips SE, Pearson AR Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Nov 1;65(Pt, 11):1088-90. Epub 2009 Oct 24. PMID:19923724[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Campeotto I, Carr SB, Trinh CH, Nelson AS, Berry A, Phillips SE, Pearson AR. Structure of an Escherichia coli N-acetyl-D-neuraminic acid lyase mutant, E192N, in complex with pyruvate at 1.45 angstrom resolution. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Nov 1;65(Pt, 11):1088-90. Epub 2009 Oct 24. PMID:19923724 doi:10.1107/S1744309109037403
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