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| | <StructureSection load='4zn0' size='340' side='right'caption='[[4zn0]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='4zn0' size='340' side='right'caption='[[4zn0]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4zn0]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Metma Metma]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZN0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZN0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4zn0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanosarcina_mazei_Go1 Methanosarcina mazei Go1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZN0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZN0 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MM_2353 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=192952 METMA])</td></tr> | + | </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=4zn0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zn0 OCA], [https://pdbe.org/4zn0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zn0 RCSB], [https://www.ebi.ac.uk/pdbsum/4zn0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zn0 ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thioredoxin-disulfide_reductase Thioredoxin-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.9 1.8.1.9] </span></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=4zn0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zn0 OCA], [http://pdbe.org/4zn0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zn0 RCSB], [http://www.ebi.ac.uk/pdbsum/4zn0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4zn0 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8PUI1_METMA Q8PUI1_METMA] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Thioredoxin Reductase|Thioredoxin Reductase]] | + | *[[Thioredoxin reductase 3D structures|Thioredoxin reductase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Metma]] | + | [[Category: Methanosarcina mazei Go1]] |
| - | [[Category: Thioredoxin-disulfide reductase]]
| + | [[Category: Balsera M]] |
| - | [[Category: Balsera, M]] | + | [[Category: Buey RM]] |
| - | [[Category: Buey, R M]] | + | [[Category: De Pereda JM]] |
| - | [[Category: Pereda, J M.de]] | + | |
| - | [[Category: Nadph]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Thioredoxin]]
| + | |
| Structural highlights
Function
Q8PUI1_METMA
Publication Abstract from PubMed
The redox regulation of proteins via reversible dithiol/disulfide exchange reactions involves the thioredoxin system, which is composed of a reductant, a thioredoxin reductase (TR), and thioredoxin (Trx). In the pyridine nucleotide-dependent Trx reduction pathway, reducing equivalents, typically from reduced nicotinamide adenine dinucleotide phosphate (NADPH), are transferred from NADPH-TR (NTR) to Trx and, in turn, to target proteins, thus resulting in the reversible modification of the structural and functional properties of the targets. NTR enzymes contain three functional sites: an NADPH binding pocket, a non-covalently bound flavin cofactor, and a redox-active disulfide in the form of CxxC. With the aim of increasing our knowledge of the thioredoxin system in archaea, we here report the high-resolution crystal structure of NTR from the methane-generating organism Methanosarcina mazei strain Go1 (MmNTR) at 2.6 A resolution. Based on the crystals presently described, MmNTR assumes an overall fold that is nearly identical to the archetypal fold of authentic NTRs; however, surprisingly, we observed no electron density for flavin adenine dinucleotide (FAD) despite the well-defined and conserved FAD-binding cavity in the folded module. Remarkably, the dimers of the apo-protein within the crystal were different from those observed by small angle X-ray scattering (SAXS) for the holo-protein, suggesting that the binding of the flavin cofactor does not require major protein structural rearrangements. Rather, binding results in the stabilization of essential parts of the structure, such as those involved in dimer stabilization. Altogether, this structure represents the example of an apo-form of an NTR that yields important insight into the effects of the cofactor on protein folding.
Crystal Structure of the Apo-Form of NADPH-Dependent Thioredoxin Reductase from a Methane-Producing Archaeon.,Buey RM, Schmitz RA, Buchanan BB, Balsera M Antioxidants (Basel). 2018 Nov 17;7(11). pii: antiox7110166. doi:, 10.3390/antiox7110166. PMID:30453601[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Buey RM, Schmitz RA, Buchanan BB, Balsera M. Crystal Structure of the Apo-Form of NADPH-Dependent Thioredoxin Reductase from a Methane-Producing Archaeon. Antioxidants (Basel). 2018 Nov 17;7(11). pii: antiox7110166. doi:, 10.3390/antiox7110166. PMID:30453601 doi:http://dx.doi.org/10.3390/antiox7110166
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