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| | <StructureSection load='4ock' size='340' side='right'caption='[[4ock]], [[Resolution|resolution]] 1.72Å' scene=''> | | <StructureSection load='4ock' size='340' side='right'caption='[[4ock]], [[Resolution|resolution]] 1.72Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4ock]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/As_1.2186 As 1.2186]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OCK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OCK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4ock]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bifidobacterium_longum Bifidobacterium longum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OCK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OCK 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></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]] 1.72Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ocj|4ocj]], [[4oco|4oco]], [[4ocp|4ocp]], [[4ocq|4ocq]], [[4ocu|4ocu]], [[4ocv|4ocv]]</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=4ock FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ock OCA], [https://pdbe.org/4ock PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ock RCSB], [https://www.ebi.ac.uk/pdbsum/4ock PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ock ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mdsC, BN57_1851 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=216816 AS 1.2186])</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=4ock FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ock OCA], [http://pdbe.org/4ock PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ock RCSB], [http://www.ebi.ac.uk/pdbsum/4ock PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ock ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/NAHK_BIFL2 NAHK_BIFL2] Phosphorylates both N-acetylglucosamine (GlcNAc) and N-acetylgalactosamine (GalNAc) at similar rates. Involved in the lacto-N-biose I/galacto-N-biose (LNB/GNB) degradation pathway, which is important for host intestinal colonization by bifidobacteria. Also accepts GTP and ITP as phosphate donors. In vitro, can phosphorylate several GlcNAc and GalNAc derivatives.<ref>PMID:17720833</ref> <ref>PMID:19436918</ref> <ref>PMID:19683921</ref> |
| | <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: As 1 2186]] | + | [[Category: Bifidobacterium longum]] |
| | [[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: Sugar binding]]
| + | |
| - | [[Category: Transferase]]
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| Structural highlights
Function
NAHK_BIFL2 Phosphorylates both N-acetylglucosamine (GlcNAc) and N-acetylgalactosamine (GalNAc) at similar rates. Involved in the lacto-N-biose I/galacto-N-biose (LNB/GNB) degradation pathway, which is important for host intestinal colonization by bifidobacteria. Also accepts GTP and ITP as phosphate donors. In vitro, can phosphorylate several GlcNAc and GalNAc derivatives.[1] [2] [3]
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[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Nishimoto M, Kitaoka M. Identification of N-acetylhexosamine 1-kinase in the complete lacto-N-biose I/galacto-N-biose metabolic pathway in Bifidobacterium longum. Appl Environ Microbiol. 2007 Oct;73(20):6444-9. Epub 2007 Aug 24. PMID:17720833 doi:http://dx.doi.org/10.1128/AEM.01425-07
- ↑ Cai L, Guan W, Kitaoka M, Shen J, Xia C, Chen W, Wang PG. A chemoenzymatic route to N-acetylglucosamine-1-phosphate analogues: substrate specificity investigations of N-acetylhexosamine 1-kinase. Chem Commun (Camb). 2009 May 28;(20):2944-6. doi: 10.1039/b904853g. Epub 2009 Apr, 24. PMID:19436918 doi:http://dx.doi.org/10.1039/b904853g
- ↑ Cai L, Guan W, Wang W, Zhao W, Kitaoka M, Shen J, O'Neil C, Wang PG. Substrate specificity of N-acetylhexosamine kinase towards N-acetylgalactosamine derivatives. Bioorg Med Chem Lett. 2009 Sep 15;19(18):5433-5. doi: 10.1016/j.bmcl.2009.07.104., Epub 2009 Jul 25. PMID:19683921 doi:http://dx.doi.org/10.1016/j.bmcl.2009.07.104
- ↑ 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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