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| | <StructureSection load='5mgy' size='340' side='right'caption='[[5mgy]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='5mgy' size='340' side='right'caption='[[5mgy]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5mgy]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_perfectomarina_atcc_14405 Pseudomonas perfectomarina atcc 14405]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MGY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MGY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5mgy]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_stutzeri_ATCC_14405_=_CCUG_16156 Pseudomonas stutzeri ATCC 14405 = CCUG 16156]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MGY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MGY FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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]] 2.6Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CXK99_00610 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=32042 Pseudomonas perfectomarina ATCC 14405])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/FAD:protein_FMN_transferase FAD:protein FMN transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.180 2.7.1.180] </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=5mgy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mgy OCA], [https://pdbe.org/5mgy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mgy RCSB], [https://www.ebi.ac.uk/pdbsum/5mgy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mgy 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=5mgy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mgy OCA], [http://pdbe.org/5mgy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mgy RCSB], [http://www.ebi.ac.uk/pdbsum/5mgy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mgy ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/A0A2N8RKH1_PSEST A0A2N8RKH1_PSEST]] Flavin transferase that catalyzes the transfer of the FMN moiety of FAD and its covalent binding to the hydroxyl group of a threonine residue in a target flavoprotein.[RuleBase:RU363002] | + | [https://www.uniprot.org/uniprot/A0A2N8RKH1_STUST A0A2N8RKH1_STUST] Flavin transferase that catalyzes the transfer of the FMN moiety of FAD and its covalent binding to the hydroxyl group of a threonine residue in a target flavoprotein.[RuleBase:RU363002] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: FAD:protein FMN transferase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pseudomonas perfectomarina atcc 14405]] | + | [[Category: Pseudomonas stutzeri ATCC 14405 = CCUG 16156]] |
| - | [[Category: Andrade, S L.A]] | + | [[Category: Andrade SLA]] |
| - | [[Category: Einsle, O]] | + | [[Category: Einsle O]] |
| - | [[Category: Trncik, C]] | + | [[Category: Trncik C]] |
| - | [[Category: Zhang, L]] | + | [[Category: Zhang L]] |
| - | [[Category: Fad binding protein flavinyl transferase]]
| + | |
| - | [[Category: Protein binding]]
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| Structural highlights
Function
A0A2N8RKH1_STUST Flavin transferase that catalyzes the transfer of the FMN moiety of FAD and its covalent binding to the hydroxyl group of a threonine residue in a target flavoprotein.[RuleBase:RU363002]
Publication Abstract from PubMed
The copper-containing enzyme nitrous oxide reductase (N2OR) catalyzes the transformation of nitrous oxide (N2O) to dinitrogen (N2) in microbial denitrification. Several accessory factors are essential for assembling the two copper sites CuA and CuZ, and for maintaining the activity. In particular, the deletion of either the transmembrane iron-sulfur flavoprotein NosR or the periplasmic protein NosX, a member of the ApbE family, abolishes N2O respiration. Here we demonstrate through biochemical and structural studies that the ApbE protein from Pseudomonas stutzeri, where the nosX gene is absent, is a monomeric FAD-binding protein that can serve as the flavin donor for NosR maturation via covalent flavinylation of a threonine residue. The flavin transfer reaction proceeds both in vivo and in vitro to generate post-translationally modified NosR with covalently bound FMN. Only FAD can act as substrate and the reaction requires a divalent cation, preferably Mg2+ that was also present in the crystal structure. In addition, the reaction is species-specific to a certain extent.
The flavinyl transferase ApbE of Pseudomonas stutzeri matures the NosR protein required for nitrous oxide reduction.,Zhang L, Trncik C, Andrade SL, Einsle O Biochim Biophys Acta. 2016 Nov 15;1858(2):95-102. doi:, 10.1016/j.bbabio.2016.11.008. PMID:27864152[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zhang L, Trncik C, Andrade SL, Einsle O. The flavinyl transferase ApbE of Pseudomonas stutzeri matures the NosR protein required for nitrous oxide reduction. Biochim Biophys Acta. 2016 Nov 15;1858(2):95-102. doi:, 10.1016/j.bbabio.2016.11.008. PMID:27864152 doi:http://dx.doi.org/10.1016/j.bbabio.2016.11.008
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