|
|
| Line 3: |
Line 3: |
| | <StructureSection load='5nck' size='340' side='right'caption='[[5nck]], [[Resolution|resolution]] 2.23Å' scene=''> | | <StructureSection load='5nck' size='340' side='right'caption='[[5nck]], [[Resolution|resolution]] 2.23Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5nck]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_fusiformis"_veillon_and_zuber_1898 "bacillus fusiformis" veillon and zuber 1898]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NCK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NCK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5nck]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Fusobacterium_nucleatum Fusobacterium nucleatum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NCK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NCK FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FN1474 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=851 "Bacillus fusiformis" Veillon and Zuber 1898])</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]] 2.23Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/N-acylmannosamine_kinase N-acylmannosamine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.60 2.7.1.60] </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=5nck FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nck OCA], [https://pdbe.org/5nck PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nck RCSB], [https://www.ebi.ac.uk/pdbsum/5nck PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nck ProSAT]</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=5nck FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nck OCA], [http://pdbe.org/5nck PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nck RCSB], [http://www.ebi.ac.uk/pdbsum/5nck PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nck ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8RDN7_FUSNN Q8RDN7_FUSNN] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 21: |
Line 22: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus fusiformis veillon and zuber 1898]] | + | [[Category: Fusobacterium nucleatum]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: N-acylmannosamine kinase]]
| + | [[Category: Caing-Carlsson R]] |
| - | [[Category: Caing-Carlsson, R]] | + | [[Category: Friemann R]] |
| - | [[Category: Friemann, R]] | + | [[Category: Ramaswamy S]] |
| - | [[Category: Ramaswamy, S]] | + | [[Category: Sharma A]] |
| - | [[Category: Sharma, A]] | + | |
| - | [[Category: N-acetylmannosamine kinase]]
| + | |
| - | [[Category: Rok family]]
| + | |
| - | [[Category: Sialic acid]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Zinc-binding motif]]
| + | |
| Structural highlights
Function
Q8RDN7_FUSNN
Publication Abstract from PubMed
Sialic acids comprise a varied group of nine-carbon amino sugars that are widely distributed among mammals and higher metazoans. Some human commensals and bacterial pathogens can scavenge sialic acids from their environment and degrade them for use as a carbon and nitrogen source. The enzyme N-acetylmannosamine kinase (NanK; EC 2.7.1.60) belongs to the transcriptional repressors, uncharacterized open reading frames and sugar kinases (ROK) superfamily. NanK catalyzes the second step of the sialic acid catabolic pathway, transferring a phosphate group from adenosine 5'-triphosphate to the C6 position of N-acetylmannosamine to generate N-acetylmannosamine 6-phosphate. The structure of NanK from Fusobacterium nucleatum was determined to 2.23 A resolution by X-ray crystallography. Unlike other NanK enzymes and ROK family members, F. nucleatum NanK does not have a conserved zinc-binding site. In spite of the absence of the zinc-binding site, all of the major structural features of enzymatic activity are conserved.
Crystal structure of N-acetylmannosamine kinase from Fusobacterium nucleatum.,Caing-Carlsson R, Goyal P, Sharma A, Ghosh S, Setty TG, North RA, Friemann R, Ramaswamy S Acta Crystallogr F Struct Biol Commun. 2017 Jun 1;73(Pt 6):356-362. doi:, 10.1107/S2053230X17007439. Epub 2017 May 31. PMID:28580924[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Caing-Carlsson R, Goyal P, Sharma A, Ghosh S, Setty TG, North RA, Friemann R, Ramaswamy S. Crystal structure of N-acetylmannosamine kinase from Fusobacterium nucleatum. Acta Crystallogr F Struct Biol Commun. 2017 Jun 1;73(Pt 6):356-362. doi:, 10.1107/S2053230X17007439. Epub 2017 May 31. PMID:28580924 doi:http://dx.doi.org/10.1107/S2053230X17007439
|
