3ngx
From Proteopedia
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| - | + | ==Crystal structure of bifunctional 5,10-methylenetetrahydrofolate dehydrogenase / cyclohydrolase from Thermoplasma acidophilum== | |
| - | + | <StructureSection load='3ngx' size='340' side='right' caption='[[3ngx]], [[Resolution|resolution]] 2.30Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[3ngx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NGX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3NGX FirstGlance]. <br> | ||
| + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ngl|3ngl]]</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ngx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ngx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ngx RCSB], [http://www.ebi.ac.uk/pdbsum/3ngx PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Folate co-enzymes play a pivotal role in one-carbon transfer cellular processes. Many eukaryotes encode the tri-functional tetrahydrofolate dehydrogenase/cyclohydrolase/synthetase (deh/cyc/syn) enzyme, which consists of a N-terminal bifunctional domain (deh/cyc) and a C-terminal monofunctional domain (syn). Here, we report the first analogous archeal enzyme structures, for the bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase from Thermoplasma acidophilum (TaMTHFDC) as the native protein and also as its NADP complex. The TaMTHFDC structure is a dimer with a polar interface, as well as a NADP binding site that shows minor conformational change. The orientations of the residues in the NADP binding site do not change on ligand binding, incorporating three water molecules which are hydrogen bonded with phosphate groups of NADP in the structure of the complex. Our structural information will contribute to an improved understanding of the basis of THF and one-carbon metabolism. | ||
| - | + | Crystal structure of bifunctional 5,10-methylenetetrahydrofolate dehydrogenase/cyclohydrolase from Thermoplasma acidophilum.,Lee WH, Sung MW, Kim JH, Kim YK, Han A, Hwang KY Biochem Biophys Res Commun. 2011 Mar 18;406(3):459-63. Epub 2011 Feb 17. PMID:21333632<ref>PMID:21333632</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | == | + | <references/> |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
[[Category: Thermoplasma acidophilum]] | [[Category: Thermoplasma acidophilum]] | ||
| - | [[Category: Hwang, K W | + | [[Category: Hwang, K W]] |
| - | [[Category: Lee, W H | + | [[Category: Lee, W H]] |
| - | [[Category: Sung, M W | + | [[Category: Sung, M W]] |
[[Category: 10-methenyltetrahydrofolate]] | [[Category: 10-methenyltetrahydrofolate]] | ||
[[Category: 10-methenyltetrahydrofolate to 10-formyltetrahydrofolate]] | [[Category: 10-methenyltetrahydrofolate to 10-formyltetrahydrofolate]] | ||
Revision as of 15:43, 18 December 2014
Crystal structure of bifunctional 5,10-methylenetetrahydrofolate dehydrogenase / cyclohydrolase from Thermoplasma acidophilum
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Categories: Thermoplasma acidophilum | Hwang, K W | Lee, W H | Sung, M W | 10-methenyltetrahydrofolate | 10-methenyltetrahydrofolate to 10-formyltetrahydrofolate | 10-methylenetetrahydrofolate to 5 | Catalyzes the oxidation of 5 | Hydrolase | Methylenetetrahydrofolate dehydrogenase/cyclohydrolase | Oxidoreductase | The hydrolysis of 5
