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

Replaces:  1D9T

Summary for 1NE7

• Entry DOI: 10.2210/pdb1ne7/pdb
• Related: 1DEA 1FS5 1FS6 1FSF 1HOR 1HOT
• Related PRD ID: PRD_900006
• Descriptor: 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)
• Functional Keywords: v-type like allosteric enzyme, conformational disorder, conformational differences, hydrolase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 6
• Total formula weight: 202375.39

Authors

Arreola, R.,Valderrama, B.,Morante, M.L.,Horjales, E. (deposition date: 2002-12-10, release date: 2003-09-23, Last modification date: 2023-08-16)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.75 Å)