4OCP

N-acetylhexosamine 1-phosphate kinase in complex with GlcNAc-1-phosphate and ADP

4OCP の概要

• エントリーDOI: 10.2210/pdb4ocp/pdb
• 関連するPDBエントリー: 4OCJ 4OCK 4OCO 4OCQ 4OCU 4OCV
• 分子名称: N-acetylhexosamine 1-phosphate kinase, 2-acetamido-2-deoxy-1-O-phosphono-alpha-D-glucopyranose, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: kinase, transferase
• 由来する生物種: Bifidobacterium longum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 43413.53

構造登録者

Li, T.L.,Wang, K.C.,Lyu, S.Y.,Liu, Y.C.,Chang, C.Y.,Wu, C.J. (登録日: 2014-01-09, 公開日: 2014-05-14, 最終更新日: 2023-12-06)

主引用文献

Wang, K.C.,Lyu, S.Y.,Liu, Y.C.,Chang, C.Y.,Wu, C.J.,Li, T.L.
Insights into the binding specificity and catalytic mechanism of N-acetylhexosamine 1-phosphate kinases through multiple reaction complexes.
Acta Crystallogr.,Sect.D, 70:1401-1410, 2014

PubMed Abstract: 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 Å. 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.

PubMed: 24816108
DOI: 10.1107/S1399004714004209

実験手法

X-RAY DIFFRACTION (1.938 Å)