2B5V

Crystal structure of glucose dehydrogenase from Haloferax mediterranei

Summary for 2B5V

• Entry DOI: 10.2210/pdb2b5v/pdb
• Related: 2B5W
• Descriptor: glucose dehydrogenase, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total)
• Functional Keywords: nucleotide binding motif, oxidoreductase
• Biological source: Haloferax mediterranei
• Total number of polymer chains: 1
• Total formula weight: 40026.13

Authors

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. (deposition date: 2005-09-29, release date: 2006-04-04, Last modification date: 2024-02-14)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2 Å)