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| | ==Crystal structure of Treponema pallidum TP0796 Flavin trafficking protein, apo form== | | ==Crystal structure of Treponema pallidum TP0796 Flavin trafficking protein, apo form== |
| - | <StructureSection load='4ifu' size='340' side='right' caption='[[4ifu]], [[Resolution|resolution]] 1.83Å' scene=''> | + | <StructureSection load='4ifu' size='340' side='right'caption='[[4ifu]], [[Resolution|resolution]] 1.83Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4ifu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Treponema_pallidum_subsp._pallidum_str._nichols Treponema pallidum subsp. pallidum str. nichols]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IFU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4IFU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4ifu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Treponema_pallidum_subsp._pallidum_str._Nichols Treponema pallidum subsp. pallidum str. Nichols]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IFU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IFU 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]] 1.8334Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">apbE, tp0796, TP_0796 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243276 Treponema pallidum subsp. pallidum str. Nichols])</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='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=4ifu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ifu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ifu RCSB], [http://www.ebi.ac.uk/pdbsum/4ifu PDBsum]</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=4ifu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ifu OCA], [https://pdbe.org/4ifu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ifu RCSB], [https://www.ebi.ac.uk/pdbsum/4ifu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ifu ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/APBE_TREPA APBE_TREPA]] 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_TREPA APBE_TREPA] 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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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 4ifu" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Treponema pallidum subsp. pallidum str. nichols]] | + | [[Category: Large Structures]] |
| - | [[Category: Brautigam, C A]] | + | [[Category: Treponema pallidum subsp. pallidum str. Nichols]] |
| - | [[Category: Deka, R K]] | + | [[Category: Brautigam CA]] |
| - | [[Category: Norgard, M V]] | + | [[Category: Deka RK]] |
| - | [[Category: Tomchick, D R]] | + | [[Category: Norgard MV]] |
| - | [[Category: Bimetal center]]
| + | [[Category: Tomchick DR]] |
| - | [[Category: Fad pyrophosphatase]]
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| - | [[Category: Flavin turnover]]
| + | |
| - | [[Category: Hydrolase]]
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| - | [[Category: Treponema pallidum]]
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| Structural highlights
Function
APBE_TREPA 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
Treponema pallidum (Tp), an obligate parasite of humans and the causative agent of syphilis, has evolved the capacity to exploit host-derived metabolites for its survival. Flavin-containing compounds are essential cofactors that are required for metabolic processes in all living organisms, and riboflavin is a direct precursor of the cofactors FMN and FAD. Unlike many pathogenic bacteria, Tp cannot synthesize riboflavin; we recently described a flavin-uptake mechanism comprised of an ABC-type transporter. However, there is a paucity of information about flavin utilization in bacterial periplasms. Using a discovery-driven approach, we have identified the TP0796 lipoprotein as a previously uncharacterized Mg2+-dependent FAD pyrophosphatase within the ApbE superfamily. TP0796 likely plays a central role in flavin turnover by hydrolyzing exogenously acquired FAD yielding AMP and FMN. Biochemical and structural investigations revealed that the enzyme has a unique bimetal Mg2+catalytic center. Furthermore, the pyrophosphatase activity is product inhibited by AMP, indicating a possible role for this molecule in modulating FMN and FAD levels in the treponemal periplasm. The ApbE superfamily was previously thought to be involved in thiamine biosynthesis, but our characterization of TP0796 prompts a re-naming of this superfamily as a periplasmic FAD processing protein (Fpp). TP0796 is the first structurally and biochemically characterized FAD pyrophosphate enzyme in bacteria. This new paradigm for a bacterial flavin-utilization pathway may prove to be useful for future inhibitor design.
The TP0796 lipoprotein of Treponema pallidum is a bimetal-dependent FAD pyrophosphatase with a potential role in flavin homeostasis.,Deka RK, Brautigam CA, Liu WZ, Tomchick DR, Norgard MV J Biol Chem. 2013 Feb 27. PMID:23447540[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. The TP0796 lipoprotein of Treponema pallidum is a bimetal-dependent FAD pyrophosphatase with a potential role in flavin homeostasis. J Biol Chem. 2013 Feb 27. PMID:23447540 doi:http://dx.doi.org/10.1074/jbc.M113.449975
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