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| | <StructureSection load='2ygy' size='340' side='right'caption='[[2ygy]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='2ygy' size='340' side='right'caption='[[2ygy]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2ygy]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecobd Ecobd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YGY OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2YGY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2ygy]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_BL21(DE3) Escherichia coli BL21(DE3)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YGY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YGY 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=CL:CHLORIDE+ION'>CL</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]] 1.9Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ygz|2ygz]], [[2wnq|2wnq]], [[2wkj|2wkj]], [[1fdz|1fdz]], [[1fdy|1fdy]], [[2wpb|2wpb]], [[2wo5|2wo5]], [[2wnn|2wnn]], [[1nal|1nal]], [[1hl2|1hl2]], [[2xfw|2xfw]], [[2wnz|2wnz]]</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=CL:CHLORIDE+ION'>CL</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=2ygy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ygy OCA], [https://pdbe.org/2ygy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ygy RCSB], [https://www.ebi.ac.uk/pdbsum/2ygy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ygy ProSAT]</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=2ygy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ygy OCA], [http://pdbe.org/2ygy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ygy RCSB], [http://www.ebi.ac.uk/pdbsum/2ygy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ygy ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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] | + | [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] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 2ygy" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 2ygy" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[N-acetylneuraminate lyase 3D structures|N-acetylneuraminate lyase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecobd]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: N-acetylneuraminate lyase]]
| + | [[Category: Berry A]] |
| - | [[Category: Berry, A]] | + | [[Category: Campeotto I]] |
| - | [[Category: Campeotto, I]] | + | [[Category: Nelson A]] |
| - | [[Category: Nelson, A]] | + | [[Category: Pearson AR]] |
| - | [[Category: Pearson, A R]] | + | [[Category: Phillips SEV]] |
| - | [[Category: Phillips, S E.V]] | + | |
| - | [[Category: Directed evolution]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Protein engineering]]
| + | |
| - | [[Category: Substrate specificity]]
| + | |
| 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]
Publication Abstract from PubMed
Twinning is a crystal growth anomaly, which has posed a challenge in macromolecular crystallography (MX) since the earliest days. Many approaches have been used to treat twinned data in order to extract structural information. However, in most cases it is usually simpler to rescreen for new crystallization conditions that yield an untwinned crystal form or, if possible, collect data from non-twinned parts of the crystal. Here, we report 11 structures of engineered variants of the E. coli enzyme N-acetyl-neuraminic lyase which, despite twinning and incommensurate modulation, have been successfully indexed, solved and deposited. These structures span a resolution range of 1.45-2.30 A, which is unusually high for datasets presenting such lattice disorders in MX and therefore these data provide an excellent test set for improving and challenging MX data processing programs.
Pathological macromolecular crystallographic data affected by twinning, partial-disorder and exhibiting multiple lattices for testing of data processing and refinement tools.,Campeotto I, Lebedev A, Schreurs AMM, Kroon-Batenburg LMJ, Lowe E, Phillips SEV, Murshudov GN, Pearson AR Sci Rep. 2018 Oct 5;8(1):14876. doi: 10.1038/s41598-018-32962-6. PMID:30291262[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Campeotto I, Lebedev A, Schreurs AMM, Kroon-Batenburg LMJ, Lowe E, Phillips SEV, Murshudov GN, Pearson AR. Pathological macromolecular crystallographic data affected by twinning, partial-disorder and exhibiting multiple lattices for testing of data processing and refinement tools. Sci Rep. 2018 Oct 5;8(1):14876. doi: 10.1038/s41598-018-32962-6. PMID:30291262 doi:http://dx.doi.org/10.1038/s41598-018-32962-6
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