View source for 4ocu


==N-acetylhexosamine 1-phosphate kinase_ATCC15697 in complex with GlcNAc==
<StructureSection load='4ocu' size='340' side='right'caption='[[4ocu]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4ocu]] 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=4OCU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OCU FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.904&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ocu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ocu OCA], [https://pdbe.org/4ocu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ocu RCSB], [https://www.ebi.ac.uk/pdbsum/4ocu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ocu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/B7GN78_BIFLS B7GN78_BIFLS] 
<div style="background-color:#fffaf0;">
== 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<ref>PMID:24816108</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4ocu" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Bifidobacterium longum subsp. infantis ATCC 15697 = JCM 1222 = DSM 20088]]
[[Category: Large Structures]]
[[Category: Chang CY]]
[[Category: Li TL]]
[[Category: Liu YC]]
[[Category: Lyu SY]]
[[Category: Wang KC]]
[[Category: Wu CJ]]