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| | <StructureSection load='5cax' size='340' side='right'caption='[[5cax]], [[Resolution|resolution]] 2.45Å' scene=''> | | <StructureSection load='5cax' size='340' side='right'caption='[[5cax]], [[Resolution|resolution]] 2.45Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5cax]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Metac Metac]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CAX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CAX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5cax]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanosarcina_acetivorans_C2A Methanosarcina acetivorans C2A]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CAX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CAX FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MA_1658 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=188937 METAC])</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=5cax FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cax OCA], [https://pdbe.org/5cax PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cax RCSB], [https://www.ebi.ac.uk/pdbsum/5cax PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cax ProSAT]</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=5cax FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cax OCA], [http://pdbe.org/5cax PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cax RCSB], [http://www.ebi.ac.uk/pdbsum/5cax PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5cax ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8TQ93_METAC Q8TQ93_METAC] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Metac]] | + | [[Category: Methanosarcina acetivorans C2A]] |
| - | [[Category: Ferry, G J]] | + | [[Category: Ferry GJ]] |
| - | [[Category: Yennawar, H P]] | + | [[Category: Yennawar HP]] |
| - | [[Category: Yennawar, N H]] | + | [[Category: Yennawar NH]] |
| - | [[Category: Coenzyme m]]
| + | |
| - | [[Category: Methanogenesis]]
| + | |
| - | [[Category: Oxidative stress]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
Q8TQ93_METAC
Publication Abstract from PubMed
Glutaredoxins (GRXs) are thiol-disulfide oxidoreductases abundant in prokaryotes, although little is understood of these enzymes from the domain Archaea. The numerous characterized GRXs from the domain Bacteria utilize a diversity of low-molecular-weight thiols in addition to glutathione as reductants. We report here the biochemical and structural properties of a GRX-like protein named methanoredoxin (MRX) from Methanosarcina acetivorans of the domain Archaea. MRX utilizes coenzyme M (CoMSH) as reductant for insulin disulfide reductase activity, which adds to the diversity of thiol protectants in prokaryotes. Cell-free extracts of M. acetivorans displayed CoMS-SCoM reductase activity that complements the CoMSH-dependent activity of MRX. The crystal structure exhibits a classic thioredoxin-glutaredoxin fold comprising three alpha-helices surrounding four antiparallel beta-sheets. A pocket on the surface contains a CVWC motif, identifying the active site with architecture similar to GRXs. Although it is a monomer in solution, the crystal lattice has four monomers in a dimer of dimers arrangement. A cadmium ion is found within the active site of each monomer. Two such ions stabilize the N-terminal tails and dimer interfaces. Our modeling studies indicate that CoMSH and glutathione (GSH) bind to the active site of MRX similar to the binding of GSH in GRXs, although there are differences in the amino acid composition of the binding motifs. The results, combined with our bioinformatic analyses, show that MRX represents a class of GRX-like enzymes present in a diversity of methane-producing Archaea.
Structural and Biochemical Characterizations of Methanoredoxin from Methanosarcina acetivorans, a Glutaredoxin-Like Enzyme with Coenzyme M-Dependent Protein Disulfide Reductase Activity.,Yenugudhati D, Prakash D, Kumar AK, Kumar RS, Yennawar NH, Yennawar HP, Ferry JG Biochemistry. 2016 Jan 19;55(2):313-21. doi: 10.1021/acs.biochem.5b00823. Epub, 2015 Dec 30. PMID:26684934[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yenugudhati D, Prakash D, Kumar AK, Kumar RS, Yennawar NH, Yennawar HP, Ferry JG. Structural and Biochemical Characterizations of Methanoredoxin from Methanosarcina acetivorans, a Glutaredoxin-Like Enzyme with Coenzyme M-Dependent Protein Disulfide Reductase Activity. Biochemistry. 2016 Jan 19;55(2):313-21. doi: 10.1021/acs.biochem.5b00823. Epub, 2015 Dec 30. PMID:26684934 doi:http://dx.doi.org/10.1021/acs.biochem.5b00823
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