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Structure determination of the glutamate dehydrogenase from the hyperthermophile Thermococcus litoralis and its comparison with that from Pyrococcus furiosus.

Abstract：

:Glutamate dehydrogenase catalyses the oxidative deamination of glutamate to 2-oxoglutarate with concomitant reduction of NAD(P)(+), and has been shown to be widely distributed in nature across species ranging from psychrophiles to hyperthermophiles. Extensive characterisation of this enzyme isolated from hyperthermophilic organisms has led to its adoption as a model system for analysing the determinants of thermal stability. The crystal structure of the extremely thermostable glutamate dehydrogenase from Thermococcus litoralis has been determined at 2.5 A resolution, and has been compared to that from the hyperthermophile Pyrococcus furiosus. The two enzymes are 87 % identical in sequence, yet differ 16-fold in their half-lives at 104 degrees C. This is the first reported comparative analysis of the structures of a multisubunit enzyme from two closely related yet distinct hyperthermophilies. The less stable T. litoralis enzyme has a decreased number of ion pair interactions; modified patterns of hydrogen bonding resulting from isosteric sequence changes; substitutions that decrease packing efficiency; and substitutions which give rise to subtle but distinct shifts in both main-chain and side-chain elements of the structure. This analysis provides a rational basis to test ideas on the factors that confer thermal stability in proteins through a combination of mutagenesis, calorimetry, and structural studies.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Britton KL,Yip KS,Sedelnikova SE,Stillman TJ,Adams MW,Ma K,Maeder DL,Robb FT,Tolliday N,Vetriani C,Rice DW,Baker PJ

doi

10.1006/jmbi.1999.3205

keywords:

subject

Has Abstract

pub_date

1999-11-12 00:00:00

pages

1121-32

issue

5

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(99)93205-9

journal_volume

293

pub_type

杂志文章

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