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| | ==Crystal structure of methylthioadenosine phosphorylase in complex with rhodamine B== | | ==Crystal structure of methylthioadenosine phosphorylase in complex with rhodamine B== |
| - | <StructureSection load='4glj' size='340' side='right' caption='[[4glj]], [[Resolution|resolution]] 1.90Å' scene=''> | + | <StructureSection load='4glj' size='340' side='right'caption='[[4glj]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4glj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Uncultivated_bacterium Uncultivated bacterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GLJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GLJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4glj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Uncultured_bacterium Uncultured bacterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GLJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GLJ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=RHB:N-[9-(2-CARBOXYPHENYL)-6-(DIETHYLAMINO)-3H-XANTHEN-3-YLIDENE]-N-ETHYLETHANAMINIUM'>RHB</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=RHB:N-[9-(2-CARBOXYPHENYL)-6-(DIETHYLAMINO)-3H-XANTHEN-3-YLIDENE]-N-ETHYLETHANAMINIUM'>RHB</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4glf|4glf]]</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=4glj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4glj OCA], [https://pdbe.org/4glj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4glj RCSB], [https://www.ebi.ac.uk/pdbsum/4glj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4glj ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rsfP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=77133 uncultivated bacterium])</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=4glj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4glj OCA], [http://pdbe.org/4glj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4glj RCSB], [http://www.ebi.ac.uk/pdbsum/4glj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4glj ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/C6KFA4_9BACT C6KFA4_9BACT]] Catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates.[HAMAP-Rule:MF_01963] | + | [https://www.uniprot.org/uniprot/C6KFA4_9BACT C6KFA4_9BACT] Catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates.[HAMAP-Rule:MF_01963] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4glj" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4glj" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[5'-deoxy-5'-methylthioadenosine phosphorylase 3D structures|5'-deoxy-5'-methylthioadenosine phosphorylase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Uncultivated bacterium]] | + | [[Category: Large Structures]] |
| - | [[Category: Bartasun, P]] | + | [[Category: Uncultured bacterium]] |
| - | [[Category: Bujacz, A]] | + | [[Category: Bartasun P]] |
| - | [[Category: Bujacz, G]] | + | [[Category: Bujacz A]] |
| - | [[Category: Cieslinski, H]] | + | [[Category: Bujacz G]] |
| - | [[Category: Antarctic soil]]
| + | [[Category: Cieslinski H]] |
| - | [[Category: Methagenomic library]]
| + | |
| - | [[Category: Methylthioadenosine]]
| + | |
| - | [[Category: Methylthioadenosine phosphorylase]]
| + | |
| - | [[Category: Rhodamine b]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
C6KFA4_9BACT Catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates.[HAMAP-Rule:MF_01963]
Publication Abstract from PubMed
The presented study examines the phenomenon of the fluorescence under UV light excitation (312 nm) of E. coli cells expressing a novel metagenomic-derived putative methylthioadenosine phosphorylase gene, called rsfp, grown on LB agar supplemented with a fluorescent dye rhodamine B. For this purpose, an rsfp gene was cloned and expressed in an LMG194 E. coli strain using an arabinose promoter. The resulting RSFP protein was purified and its UV-VIS absorbance spectrum and emission spectrum were assayed. Simultaneously, the same spectroscopic studies were carried out for rhodamine B in the absence or presence of RSFP protein or native E. coli proteins, respectively. The results of the spectroscopic studies suggested that the fluorescence of E. coli cells expressing rsfp gene under UV illumination is due to the interaction of rhodamine B molecules with the RSFP protein. Finally, this interaction was proved by a crystallographic study and then by site-directed mutagenesis of rsfp gene sequence. The crystal structures of RSFP apo form (1.98 A) and complex RSFP/RB (1.90 A) show a trimer of RSFP molecules located on the crystallographic six fold screw axis. The RSFP complex with rhodamine B revealed the binding site for RB, in the pocket located on the interface between symmetry related monomers.
A study on the interaction of rhodamine B with methylthioadenosine phosphorylase protein sourced from an antarctic soil metagenomic library.,Bartasun P, Cieslinski H, Bujacz A, Wierzbicka-Wos A, Kur J PLoS One. 2013;8(1):e55697. doi: 10.1371/journal.pone.0055697. Epub 2013 Jan 31. PMID:23383268[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bartasun P, Cieslinski H, Bujacz A, Wierzbicka-Wos A, Kur J. A study on the interaction of rhodamine B with methylthioadenosine phosphorylase protein sourced from an antarctic soil metagenomic library. PLoS One. 2013;8(1):e55697. doi: 10.1371/journal.pone.0055697. Epub 2013 Jan 31. PMID:23383268 doi:http://dx.doi.org/10.1371/journal.pone.0055697
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