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| | <StructureSection load='4ocv' size='340' side='right'caption='[[4ocv]], [[Resolution|resolution]] 1.47Å' scene=''> | | <StructureSection load='4ocv' size='340' side='right'caption='[[4ocv]], [[Resolution|resolution]] 1.47Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4ocv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bifls Bifls]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OCV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OCV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4ocv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bifidobacterium_longum_subsp._infantis_ATCC_15697_=_JCM_1222_=_DSM_20088 Bifidobacterium longum subsp. infantis ATCC 15697 = JCM 1222 = DSM 20088]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OCV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OCV FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</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]] 1.472Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ocj|4ocj]], [[4ock|4ock]], [[4oco|4oco]], [[4ocp|4ocp]], [[4ocq|4ocq]], [[4ocu|4ocu]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</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">BLIJ_2250, Blon_2173 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=391904 BIFLS])</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=4ocv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ocv OCA], [https://pdbe.org/4ocv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ocv RCSB], [https://www.ebi.ac.uk/pdbsum/4ocv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ocv 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-acetylhexosamine_1-kinase N-acetylhexosamine 1-kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.162 2.7.1.162] </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=4ocv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ocv OCA], [http://pdbe.org/4ocv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ocv RCSB], [http://www.ebi.ac.uk/pdbsum/4ocv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ocv ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/B7GN78_BIFLS B7GN78_BIFLS] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bifls]] | + | [[Category: Bifidobacterium longum subsp. infantis ATCC 15697 = JCM 1222 = DSM 20088]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: N-acetylhexosamine 1-kinase]]
| + | [[Category: Chang CY]] |
| - | [[Category: Chang, C Y]] | + | [[Category: Li TL]] |
| - | [[Category: Li, T L]] | + | [[Category: Liu YC]] |
| - | [[Category: Liu, Y C]] | + | [[Category: Lyu SY]] |
| - | [[Category: Lyu, S Y]] | + | [[Category: Wang KC]] |
| - | [[Category: Wang, K C]] | + | [[Category: Wu CJ]] |
| - | [[Category: Wu, C J]] | + | |
| - | [[Category: Kinase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
B7GN78_BIFLS
Publication Abstract from PubMed
Utilization of N-acetylhexosamine in bifidobacteria requires the specific lacto-N-biose/galacto-N-biose pathway, a pathway differing from the Leloir pathway while establishing symbiosis between humans and bifidobacteria. The gene lnpB in the pathway encodes a novel hexosamine kinase NahK, which catalyzes the formation of N-acetylhexosamine 1-phosphate (GlcNAc-1P/GalNAc-1P). In this report, seven three-dimensional structures of NahK in complex with GlcNAc, GalNAc, GlcNAc-1P, GlcNAc/AMPPNP and GlcNAc-1P/ADP from both Bifidobacterium longum (JCM1217) and B. infantis (ATCC15697) were solved at resolutions of 1.5-2.2 A. NahK is a monomer in solution, and its polypeptide folds in a crescent-like architecture subdivided into two domains by a deep cleft. The NahK structures presented here represent the first multiple reaction complexes of the enzyme. This structural information reveals the molecular basis for the recognition of the given substrates and products, GlcNAc/GalNAc, GlcNAc-1P/GalNAc-1P, ATP/ADP and Mg(2+), and provides insights into the catalytic mechanism, enabling NahK and mutants thereof to form a choice of biocatalysts for enzymatic and chemoenzymatic synthesis of carbohydrates.
Insights into the binding specificity and catalytic mechanism of N-acetylhexosamine 1-phosphate kinases through multiple reaction complexes.,Wang KC, Lyu SY, Liu YC, Chang CY, Wu CJ, Li TL Acta Crystallogr D Biol Crystallogr. 2014 May;70(Pt 5):1401-10. doi:, 10.1107/S1399004714004209. Epub 2014 Apr 30. PMID:24816108[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wang KC, Lyu SY, Liu YC, Chang CY, Wu CJ, Li TL. Insights into the binding specificity and catalytic mechanism of N-acetylhexosamine 1-phosphate kinases through multiple reaction complexes. Acta Crystallogr D Biol Crystallogr. 2014 May;70(Pt 5):1401-10. doi:, 10.1107/S1399004714004209. Epub 2014 Apr 30. PMID:24816108 doi:http://dx.doi.org/10.1107/S1399004714004209
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