1hdg: Difference between revisions
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|PDB= 1hdg |SIZE=350|CAPTION= <scene name='initialview01'>1hdg</scene>, resolution 2.5Å | |PDB= 1hdg |SIZE=350|CAPTION= <scene name='initialview01'>1hdg</scene>, resolution 2.5Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Glyceraldehyde-3-phosphate_dehydrogenase_(phosphorylating) Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.12 1.2.1.12] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glyceraldehyde-3-phosphate_dehydrogenase_(phosphorylating) Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.12 1.2.1.12] </span> | ||
|GENE= TN10 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 Thermotoga maritima]) | |GENE= TN10 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 Thermotoga maritima]) | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hdg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hdg OCA], [http://www.ebi.ac.uk/pdbsum/1hdg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hdg RCSB]</span> | |||
}} | }} | ||
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[[Category: Steipe, B.]] | [[Category: Steipe, B.]] | ||
[[Category: Tomschy, A.]] | [[Category: Tomschy, A.]] | ||
[[Category: oxidoreductase (aldehy(d)-nad(a))]] | [[Category: oxidoreductase (aldehy(d)-nad(a))]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:02:57 2008'' | ||
Revision as of 18:03, 30 March 2008
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| 1hdg, resolution 2.5Å | |||||||||||||
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| Ligands: | NAD, SO4 | ||||||||||||
| Gene: | TN10 (Thermotoga maritima) | ||||||||||||
| Activity: | Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating), with EC number 1.2.1.12 | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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. 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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