3ngl

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Current revision (10:00, 14 February 2024) (edit) (undo)
 
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<StructureSection load='3ngl' size='340' side='right'caption='[[3ngl]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='3ngl' size='340' side='right'caption='[[3ngl]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3ngl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"thermoplasma_acidophila"_(sic)_darland_et_al._1970 "thermoplasma acidophila" (sic) darland et al. 1970]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NGL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NGL FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3ngl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NGL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NGL FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ngx|3ngx]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></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=3ngl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ngl OCA], [https://pdbe.org/3ngl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ngl RCSB], [https://www.ebi.ac.uk/pdbsum/3ngl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ngl ProSAT]</span></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=3ngl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ngl OCA], [https://pdbe.org/3ngl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ngl RCSB], [https://www.ebi.ac.uk/pdbsum/3ngl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ngl ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/FOLD_THEAC FOLD_THEAC]] Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate (By similarity).
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[https://www.uniprot.org/uniprot/FOLD_THEAC FOLD_THEAC] Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate (By similarity).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3ngl" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Hwang, K Y]]
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[[Category: Thermoplasma acidophilum]]
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[[Category: Lee, W H]]
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[[Category: Hwang KY]]
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[[Category: Sung, M W]]
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[[Category: Lee WH]]
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[[Category: 10-methenyltetrahydrofolate]]
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[[Category: Sung MW]]
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[[Category: 10-methenyltetrahydrofolate to 10-formyltetrahydrofolate]]
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[[Category: 10-methylenetetrahydrofolate to 5]]
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[[Category: Catalyzes the oxidation of 5]]
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[[Category: Hydrolase]]
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[[Category: Methylenetetrahydrofolate dehydrogenase/cyclohydrolase]]
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[[Category: Oxidoreductase]]
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[[Category: The hydrolysis of 5]]
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Current revision

Crystal structure of bifunctional 5,10-methylenetetrahydrofolate dehydrogenase / cyclohydrolase from Thermoplasma acidophilum

PDB ID 3ngl

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