Max-Planck Institut fur Biochemie, Martinsried, FRG.
J Mol Biol 246: 511-21 (1995)
Abstract
The crystal structure of holo-glyceraldehyde-3-phosphate dehydrogenase
from the hyperthermophile Thermotoga maritima was determined by
Patterson search methods using the known structure of the Bacillus
stearothermophilus enzyme. The structure was refined at a resolution of
2.5 A to an R-factor of 16.63% for 26289 reflections between 8.0 A an
2.5 A with F > 2 sigma(F). The crystallographic asymmetric unit contains
two monomers related by approximate 2-fold symmetry and a tetramer is
built up by crystallographic symmetry. The root-mean-square deviation of
Ca positions of glyceraldehyde-3-phosphate dehydrogenase from T.
maritima and B. stearothermophilus is 0.83 A in the NAD+ binding domains
and smaller close to the cofactor. In contrast, the largest deviations
in the catalytic domains are found at residues involved in coordination
of sulphate ion SO4 339, which most likely marks the site of the
attacking inorganic phosphate ion in catalysis. A large number of extra
salt-bridges may be an important factor contributing to the high
thermostability of this protein.
Mesh Headings
Unique Identifier: 95182459
Chemical Identifiers (Names)