2B5V

Crystal structure of glucose dehydrogenase from Haloferax mediterranei

2B5V の概要

• エントリーDOI: 10.2210/pdb2b5v/pdb
• 関連するPDBエントリー: 2B5W
• 分子名称: glucose dehydrogenase, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total)
• 機能のキーワード: nucleotide binding motif, oxidoreductase
• 由来する生物種: Haloferax mediterranei
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 40026.13

構造登録者

Britton, K.L.,Baker, P.J.,Fisher, M.,Ruzheinikov, S.,Gilmour, D.J.,Bonete, M.-J.,Ferrer, J.,Pire, C.,Esclapez, J.,Rice, D.W. (登録日: 2005-09-29, 公開日: 2006-04-04, 最終更新日: 2024-02-14)

主引用文献

Britton, K.L.,Baker, P.J.,Fisher, M.,Ruzheinikov, S.,Gilmour, D.J.,Bonete, M.-J.,Ferrer, J.,Pire, C.,Esclapez, J.,Rice, D.W.
Analysis of protein solvent interactions in glucose dehydrogenase from the extreme halophile Haloferax mediterranei.
Proc.Natl.Acad.Sci.Usa, 103:4846-4851, 2006

PubMed Abstract: The structure of glucose dehydrogenase from the extreme halophile Haloferax mediterranei has been solved at 1.6-A resolution under crystallization conditions which closely mimic the "in vivo" intracellular environment. The decoration of the enzyme's surface with acidic residues is only partially neutralized by bound potassium counterions, which also appear to play a role in substrate binding. The surface shows the expected reduction in hydrophobic character, surprisingly not from changes associated with the loss of exposed hydrophobic residues but rather arising from a loss of lysines consistent with the genome wide-reduction of this residue in extreme halophiles. The structure reveals a highly ordered, multilayered solvation shell that can be seen to be organized into one dominant network covering much of the exposed surface accessible area to an extent not seen in almost any other protein structure solved. This finding is consistent with the requirement of the enzyme to form a protective shell in a dehydrating environment.

PubMed: 16551747
DOI: 10.1073/pnas.0508854103

実験手法

X-RAY DIFFRACTION (2 Å)