1NE7

HUMAN GLUCOSAMINE-6-PHOSPHATE DEAMINASE ISOMERASE AT 1.75 A RESOLUTION COMPLEXED WITH N-ACETYL-GLUCOSAMINE-6-PHOSPHATE AND 2-DEOXY-2-AMINO-GLUCITOL-6-PHOSPHATE

「1D9T」から置き換えられました

1NE7 の概要

• エントリーDOI: 10.2210/pdb1ne7/pdb
• 関連するPDBエントリー: 1DEA 1FS5 1FS6 1FSF 1HOR 1HOT
• 関連するBIRD辞書のPRD_ID: PRD_900006
• 分子名称: Glucosamine-6-phosphate isomerase, alpha-D-glucopyranose-(1-1)-alpha-D-glucopyranose, 2-acetamido-2-deoxy-6-O-phosphono-alpha-D-glucopyranose, ... (6 entities in total)
• 機能のキーワード: v-type like allosteric enzyme, conformational disorder, conformational differences, hydrolase
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 202375.39

構造登録者

Arreola, R.,Valderrama, B.,Morante, M.L.,Horjales, E. (登録日: 2002-12-10, 公開日: 2003-09-23, 最終更新日: 2023-08-16)

主引用文献

Arreola, R.,Valderrama, B.,Morante, M.L.,Horjales, E.
Two mammalian glucosamine-6-phosphate deaminases: a structural and genetic study.
Febs Lett., 551:63-70, 2003

PubMed Abstract: Glucosamine-6-phosphate deaminase (EC 3.5.99.6) is an allosteric enzyme that catalyzes the reversible conversion of D-glucosamine-6-phosphate into D-fructose-6-phosphate and ammonium. Here we describe the existence of two mammalian glucosamine-6-phosphate deaminase enzymes. We present the crystallographic structure of one of them, the long human glucosamine-6-phosphate deaminase, at 1.75 A resolution. Crystals belong to the space group P2(1)2(1)2(1) and present a whole hexamer in the asymmetric unit. The active-site lid (residues 162-182) presented significant structural differences among monomers. Interestingly the region with the largest differences, when compared with the Escherichia coli homologue, was found to be close to the active site. These structural differences can be related to the kinetic and allosteric properties of both mammalian enzymes.

PubMed: 12965206
DOI: 10.1016/S0014-5793(03)00896-2

実験手法

X-RAY DIFFRACTION (1.75 Å)