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| | <StructureSection load='1b0a' size='340' side='right'caption='[[1b0a]], [[Resolution|resolution]] 2.56Å' scene=''> | | <StructureSection load='1b0a' size='340' side='right'caption='[[1b0a]], [[Resolution|resolution]] 2.56Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1b0a]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B0A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1B0A FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1b0a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B0A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B0A FirstGlance]. <br> |
| - | </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=1b0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b0a OCA], [http://pdbe.org/1b0a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1b0a RCSB], [http://www.ebi.ac.uk/pdbsum/1b0a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1b0a ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.56Å</td></tr> |
| | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1b0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b0a OCA], [https://pdbe.org/1b0a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b0a RCSB], [https://www.ebi.ac.uk/pdbsum/1b0a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b0a ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/FOLD_ECOLI FOLD_ECOLI]] Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate. This enzyme is specific for NADP.<ref>PMID:1748668</ref> | + | [https://www.uniprot.org/uniprot/FOLD_ECOLI FOLD_ECOLI] Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate. This enzyme is specific for NADP.<ref>PMID:1748668</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Escherichia coli K-12]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ari, L D]] | + | [[Category: D'Ari L]] |
| - | [[Category: Dyer, D]] | + | [[Category: Dyer D]] |
| - | [[Category: Huang, J Y]] | + | [[Category: Huang J-Y]] |
| - | [[Category: Rabinowitz, J]] | + | [[Category: Rabinowitz J]] |
| - | [[Category: Shen, B W]] | + | [[Category: Shen BW]] |
| - | [[Category: Stoddard, B L]] | + | [[Category: Stoddard BL]] |
| - | [[Category: Bifunctional]]
| + | |
| - | [[Category: Channeling]]
| + | |
| - | [[Category: Cyclcohydrolase]]
| + | |
| - | [[Category: Dehydrogenase]]
| + | |
| - | [[Category: Folate]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
FOLD_ECOLI Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate. This enzyme is specific for NADP.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The structure of a bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/cyclohydrolase from Escherichia coli has been determined at 2.5 A resolution in the absence of bound substrates and compared to the NADP-bound structure of the homologous enzyme domains from a trifunctional human synthetase enzyme. Superposition of these structures allows the identification of a highly conserved cluster of basic residues that are appropriately positioned to serve as a binding site for the poly-gamma-glutamyl tail of the tetrahydrofolate substrate. Modeling studies and molecular dynamic simulations of bound methylene-tetrahydrofolate and NADP shows that this binding site would allow interaction of the nicotinamide and pterin rings in the dehydrogenase active site. Comparison of these enzymes also indicates differences between their active sites that might allow the development of inhibitors specific to the bacterial target.
The crystal structure of a bacterial, bifunctional 5,10 methylene-tetrahydrofolate dehydrogenase/cyclohydrolase.,Shen BW, Dyer DH, Huang JY, D'Ari L, Rabinowitz J, Stoddard BL Protein Sci. 1999 Jun;8(6):1342-9. PMID:10386884[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ D'Ari L, Rabinowitz JC. Purification, characterization, cloning, and amino acid sequence of the bifunctional enzyme 5,10-methylenetetrahydrofolate dehydrogenase/5,10-methenyltetrahydrofolate cyclohydrolase from Escherichia coli. J Biol Chem. 1991 Dec 15;266(35):23953-8. PMID:1748668
- ↑ Shen BW, Dyer DH, Huang JY, D'Ari L, Rabinowitz J, Stoddard BL. The crystal structure of a bacterial, bifunctional 5,10 methylene-tetrahydrofolate dehydrogenase/cyclohydrolase. Protein Sci. 1999 Jun;8(6):1342-9. PMID:10386884
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