2dtd
From Proteopedia
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|PDB= 2dtd |SIZE=350|CAPTION= <scene name='initialview01'>2dtd</scene>, resolution 2.10Å | |PDB= 2dtd |SIZE=350|CAPTION= <scene name='initialview01'>2dtd</scene>, resolution 2.10Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Glucose_1-dehydrogenase_(NAD(+)) Glucose 1-dehydrogenase (NAD(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.118 1.1.1.118] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucose_1-dehydrogenase_(NAD(+)) Glucose 1-dehydrogenase (NAD(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.118 1.1.1.118] </span> |
|GENE= Ta0754 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2303 Thermoplasma acidophilum]) | |GENE= Ta0754 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2303 Thermoplasma acidophilum]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2dte|2dte]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2dtd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dtd OCA], [http://www.ebi.ac.uk/pdbsum/2dtd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2dtd RCSB]</span> | ||
}} | }} | ||
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[[Category: Tamura, T.]] | [[Category: Tamura, T.]] | ||
[[Category: Yasutake, Y.]] | [[Category: Yasutake, Y.]] | ||
| - | [[Category: SO4]] | ||
[[Category: rossmann fold]] | [[Category: rossmann fold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:39:16 2008'' |
Revision as of 23:39, 30 March 2008
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| , resolution 2.10Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | Ta0754 (Thermoplasma acidophilum) | ||||||
| Activity: | Glucose 1-dehydrogenase (NAD(+)), with EC number 1.1.1.118 | ||||||
| Related: | 2dte
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of Thermoplasma acidophilum aldohexose dehydrogenase (AldT) in ligand-free form
Overview
The D-aldohexose dehydrogenase from the thermoacidophilic archaea Thermoplasma acidophilum (AldT) belongs to the short-chain dehydrogenase/reductase (SDR) superfamily and catalyzes the oxidation of several monosaccharides with a preference for NAD(+) rather than NADP(+) as a cofactor. It has been found that AldT is a unique enzyme that exhibits the highest dehydrogenase activity against D-mannose. Here, we describe the crystal structures of AldT in ligand-free form, in complex with NADH, and in complex with the substrate D-mannose, at 2.1 A, 1.65 A, and 1.6 A resolution, respectively. The AldT subunit forms a typical SDR fold with an unexpectedly long C-terminal tail and assembles into an intertwined tetramer. The D-mannose complex structure reveals that Glu84 interacts with the axial C2 hydroxyl group of the bound D-mannose. Structural comparison with Bacillus megaterium glucose dehydrogenase (BmGlcDH) suggests that the conformation of the glutamate side-chain is crucial for discrimination between D-mannose and its C2 epimer D-glucose, and the conformation of the glutamate side-chain depends on the spatial arrangement of nearby hydrophobic residues that do not directly interact with the substrate. Elucidation of the D-mannose recognition mechanism of AldT further provides structural insights into the unique substrate selectivity of AldT. Finally, we show that the extended C-terminal tail completely shuts the substrate-binding pocket of the neighboring subunit both in the presence and absence of substrate. The elaborate inter-subunit interactions between the C-terminal tail and the entrance of the substrate-binding pocket imply that the tail may play a pivotal role in the enzyme activity.
About this Structure
2DTD is a Single protein structure of sequence from Thermoplasma acidophilum. Full crystallographic information is available from OCA.
Reference
Structural insights into unique substrate selectivity of Thermoplasma acidophilum D-aldohexose dehydrogenase., Yasutake Y, Nishiya Y, Tamura N, Tamura T, J Mol Biol. 2007 Apr 6;367(4):1034-46. Epub 2007 Jan 16. PMID:17300803
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