2o2q
From Proteopedia
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|PDB= 2o2q |SIZE=350|CAPTION= <scene name='initialview01'>2o2q</scene>, resolution 2.00Å | |PDB= 2o2q |SIZE=350|CAPTION= <scene name='initialview01'>2o2q</scene>, resolution 2.00Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Formyltetrahydrofolate_dehydrogenase Formyltetrahydrofolate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.6 1.5.1.6] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Formyltetrahydrofolate_dehydrogenase Formyltetrahydrofolate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.6 1.5.1.6] </span> |
|GENE= Fthfd ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | |GENE= Fthfd ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2o2p|2O2P]], [[2o2r|2O2R]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2o2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o2q OCA], [http://www.ebi.ac.uk/pdbsum/2o2q PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2o2q RCSB]</span> | ||
}} | }} | ||
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[[Category: Krupenko, S A.]] | [[Category: Krupenko, S A.]] | ||
[[Category: Tsybovsky, Y.]] | [[Category: Tsybovsky, Y.]] | ||
| - | [[Category: GOL]] | ||
| - | [[Category: MG]] | ||
| - | [[Category: NAP]] | ||
| - | [[Category: SO4]] | ||
[[Category: aldehyde dehydrogenase]] | [[Category: aldehyde dehydrogenase]] | ||
[[Category: fdh]] | [[Category: fdh]] | ||
| - | ''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 04:11:53 2008'' |
Revision as of 01:11, 31 March 2008
| |||||||
| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Gene: | Fthfd (Rattus norvegicus) | ||||||
| Activity: | Formyltetrahydrofolate dehydrogenase, with EC number 1.5.1.6 | ||||||
| Related: | 2O2P, 2O2R
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the C-terminal domain of rat 10'formyltetrahydrofolate dehydrogenase in complex with NADP
Overview
10-Formyltetrahydrofolate dehydrogenase (FDH) catalyzes an NADP+-dependent dehydrogenase reaction resulting in conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. This reaction is a result of the concerted action of two catalytic domains of FDH, the amino-terminal hydrolase domain and the carboxyl-terminal aldehyde dehydrogenase domain. In addition to participation in the overall FDH mechanism, the C-terminal domain is capable of NADP+-dependent oxidation of short chain aldehydes to their corresponding acids. We have determined the crystal structure of the C-terminal domain of FDH and its complexes with oxidized and reduced forms of NADP. Compared to other members of the ALDH family, FDH demonstrates a new mode of binding of the 2'-phosphate group of NADP via a water-mediated contact with Gln600 that may contribute to the specificity of the enzyme for NADP over NAD. The structures also suggest how Glu673 can act as a general base in both acylation and deacylation steps of the reaction. In the apo structure, the general base Glu673 is positioned optimally for proton abstraction from the sulfur atom of Cys707. Upon binding of NADP+, the side chain of Glu673 is displaced from the active site by the nicotinamide ring and contacts a chain of highly ordered water molecules that may represent a pathway for translocation of the abstracted proton from Glu673 to the solvent. When reduced, the nicotinamide ring of NADP is displaced from the active site, restoring the contact between Cys707 and Glu673 and allowing the latter to activate the hydrolytic water molecule in deacylation.
About this Structure
2O2Q is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Crystal structures of the carboxyl terminal domain of rat 10-formyltetrahydrofolate dehydrogenase: implications for the catalytic mechanism of aldehyde dehydrogenases., Tsybovsky Y, Donato H, Krupenko NI, Davies C, Krupenko SA, Biochemistry. 2007 Mar 20;46(11):2917-29. Epub 2007 Feb 16. PMID:17302434
Page seeded by OCA on Mon Mar 31 04:11:53 2008
