1hdg
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(New page: 200px<br /><applet load="1hdg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hdg, resolution 2.5Å" /> '''THE CRYSTAL STRUCTURE...)
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Revision as of 14:25, 20 November 2007
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THE CRYSTAL STRUCTURE OF HOLO-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE FROM THE HYPERTHERMOPHILIC BACTERIUM THERMOTOGA MARITIMA AT 2.5 ANGSTROMS RESOLUTION
Overview
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.
About this Structure
1HDG is a Single protein structure of sequence from Thermotoga maritima with SO4 and NAD as ligands. Active as Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating), with EC number 1.2.1.12 Full crystallographic information is available from OCA.
Reference
The crystal structure of holo-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima at 2.5 A resolution., Korndorfer I, Steipe B, Huber R, Tomschy A, Jaenicke R, J Mol Biol. 1995 Mar 3;246(4):511-21. PMID:7877172
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