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| | ==Crystal structure of Escherichia coli Flavin trafficking protein, an FMN transferase, Y60N mutant, ADP-inhibited== | | ==Crystal structure of Escherichia coli Flavin trafficking protein, an FMN transferase, Y60N mutant, ADP-inhibited== |
| - | <StructureSection load='4xgx' size='340' side='right' caption='[[4xgx]], [[Resolution|resolution]] 1.90Å' scene=''> | + | <StructureSection load='4xgx' size='340' side='right'caption='[[4xgx]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4xgx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XGX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XGX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4xgx]] is a 2 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=4XGX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XGX FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4xgv|4xgv]]</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=4xgx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xgx OCA], [https://pdbe.org/4xgx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xgx RCSB], [https://www.ebi.ac.uk/pdbsum/4xgx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xgx ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">apbE, yojK, yojL, b2214, JW5368 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4xgx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xgx OCA], [http://pdbe.org/4xgx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xgx RCSB], [http://www.ebi.ac.uk/pdbsum/4xgx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xgx ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/APBE_ECOLI APBE_ECOLI]] Involved in the conversion of aminoimidazole ribotide (AIR), a purine intermediate, to the 4-amino-5-hydroxymethyl-2-methyl pyrimidine (HMP) moiety of thiamine (By similarity). | + | [https://www.uniprot.org/uniprot/APBE_ECOLI APBE_ECOLI] Involved in the conversion of aminoimidazole ribotide (AIR), a purine intermediate, to the 4-amino-5-hydroxymethyl-2-methyl pyrimidine (HMP) moiety of thiamine (By similarity). |
| | <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: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: FAD:protein FMN transferase]] | + | [[Category: Large Structures]] |
| - | [[Category: Brautigam, C A]] | + | [[Category: Brautigam CA]] |
| - | [[Category: Deka, R K]] | + | [[Category: Deka RK]] |
| - | [[Category: Norgard, M V]] | + | [[Category: Norgard MV]] |
| - | [[Category: Tomchick, D R]] | + | [[Category: Tomchick DR]] |
| - | [[Category: Bimetal center]]
| + | |
| - | [[Category: Flavin transferase]]
| + | |
| - | [[Category: Lipoprotein]]
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| - | [[Category: Transferase-transferase inhibitor complex]]
| + | |
| Structural highlights
Function
APBE_ECOLI Involved in the conversion of aminoimidazole ribotide (AIR), a purine intermediate, to the 4-amino-5-hydroxymethyl-2-methyl pyrimidine (HMP) moiety of thiamine (By similarity).
Publication Abstract from PubMed
We recently reported a flavin-trafficking protein (Ftp) in the syphilis spirochete Treponema pallidum (Ftp_Tp) as the first bacterial metal-dependent FAD pyrophosphatase that hydrolyzes FAD into AMP and FMN in the periplasm. Orthologs of Ftp_Tp in other bacteria (formerly ApbE) appear to lack this hydrolytic activity; rather, they flavinylate the redox subunit, NqrC, via their metal-dependent FMN transferase activity. However, nothing has been known about the nature or mechanism of metal-dependent Ftp catalysis in either Nqr- or Rnf-redox-containing bacteria. In the current study, we identified a bimetal center in the crystal structure of Escherichia coli Ftp (Ftp_Ec) and show via mutagenesis that a single amino acid substitution converts it from an FAD-binding protein to a Mg2+ -dependent FAD pyrophosphatase (Ftp_Tp-like). Furthermore, in the presence of protein substrates, both types of Ftps are capable of flavinylating periplasmic redox-carrying proteins (e.g., RnfG_Ec) via the metal-dependent covalent attachment of FMN. A high-resolution structure of the Ftp-mediated flavinylated protein of Shewanella oneidensis NqrC identified an essential lysine in phosphoester-threonyl-FMN bond formation in the posttranslationally modified flavoproteins. Together, these discoveries broaden our understanding of the physiological capabilities of the bacterial periplasm, and they also clarify a possible mechanism by which flavoproteins are generated.
Molecular insights into the enzymatic diversity of flavin-trafficking protein (Ftp; formerly ApbE) in flavoprotein biogenesis in the bacterial periplasm.,Deka RK, Brautigam CA, Liu WZ, Tomchick DR, Norgard MV Microbiologyopen. 2015 Dec 2. doi: 10.1002/mbo3.306. PMID:26626129[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Deka RK, Brautigam CA, Liu WZ, Tomchick DR, Norgard MV. Molecular insights into the enzymatic diversity of flavin-trafficking protein (Ftp; formerly ApbE) in flavoprotein biogenesis in the bacterial periplasm. Microbiologyopen. 2015 Dec 2. doi: 10.1002/mbo3.306. PMID:26626129 doi:http://dx.doi.org/10.1002/mbo3.306
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