1hdg

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[[Image:1hdg.jpg|left|200px]]<br /><applet load="1hdg" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1hdg.jpg|left|200px]]
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caption="1hdg, resolution 2.5&Aring;" />
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'''THE CRYSTAL STRUCTURE OF HOLO-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE FROM THE HYPERTHERMOPHILIC BACTERIUM THERMOTOGA MARITIMA AT 2.5 ANGSTROMS RESOLUTION'''<br />
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{{Structure
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|PDB= 1hdg |SIZE=350|CAPTION= <scene name='initialview01'>1hdg</scene>, resolution 2.5&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>
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|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]
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|GENE= TN10 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 Thermotoga maritima])
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}}
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'''THE CRYSTAL STRUCTURE OF HOLO-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE FROM THE HYPERTHERMOPHILIC BACTERIUM THERMOTOGA MARITIMA AT 2.5 ANGSTROMS RESOLUTION'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1HDG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=NAD:'>NAD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HDG OCA].
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1HDG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HDG OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7877172 7877172]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/7877172 7877172]
[[Category: Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)]]
[[Category: Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: oxidoreductase (aldehy(d)-nad(a))]]
[[Category: oxidoreductase (aldehy(d)-nad(a))]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:00:10 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:35:43 2008''

Revision as of 09:35, 20 March 2008


PDB ID 1hdg

Drag the structure with the mouse to rotate
, resolution 2.5Å
Ligands: and
Gene: TN10 (Thermotoga maritima)
Activity: Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating), with EC number 1.2.1.12
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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