Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3WIE

Structure of a glucose dehydrogenase T277F mutant in complex with D-glucose and NAADP

Summary for 3WIE
Entry DOI10.2210/pdb3wie/pdb
Related3WIC 3WID
DescriptorGlucose 1-dehydrogenase, ZINC ION, [[(2R,3R,4R,5R)-5-(6-aminopurin-9-yl)-3-oxidanyl-4-phosphonooxy-oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(2R,3S,4R,5R)-5-(3-carboxypyridin-1-ium-1-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl phosphate, ... (5 entities in total)
Functional Keywordsrossmann fold, oxidoreductase
Biological sourceThermoplasma volcanium
Total number of polymer chains4
Total formula weight169877.91
Authors
Sakuraba, H.,Kanoh, Y.,Yoneda, K.,Ohshima, T. (deposition date: 2013-09-10, release date: 2014-05-14, Last modification date: 2023-11-08)
Primary citationKanoh, Y.,Uehara, S.,Iwata, H.,Yoneda, K.,Ohshima, T.,Sakuraba, H.
Structural insight into glucose dehydrogenase from the thermoacidophilic archaeon Thermoplasma volcanium.
Acta Crystallogr.,Sect.D, 70:1271-1280, 2014
Cited by
PubMed Abstract: Glucose dehydrogenase from the thermoacidophilic archaeon Thermoplasma volcanium (tvGlcDH) is highly active towards D-glucose and D-galactose, but does not utilize aldopentoses such as D-xylose as substrates. In the present study, the crystal structures of substrate/cofactor-free tvGlcDH and of a tvGlcDH T277F mutant in a binary complex with NADP and in a ternary complex with D-glucose and nicotinic acid adenine dinucleotide phosphate, an NADP analogue, were determined at resolutions of 2.6, 2.25 and 2.33 Å, respectively. The overall structure of each monomer showed notable similarity to that of the enzyme from Sulfolobus solfataricus (ssGlcDH-1), which accepts a broad range of C5 and C6 sugars as substrates. However, the amino-acid residues of tvGlcDH involved in substrate binding markedly differed from those of ssGlcDH-1. Structural comparison revealed that a decreased number of interactions between the C3-hydroxyl group of the sugar and the enzyme are likely to be responsible for the lack of reactivity of tvGlcDH towards D-xylose.
PubMed: 24816096
DOI: 10.1107/S1399004714002363
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.33 Å)
Structure validation

226707

건을2024-10-30부터공개중

PDB statisticsPDBj update infoContact PDBjnumon