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| | <StructureSection load='1jdu' size='340' side='right'caption='[[1jdu]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='1jdu' size='340' side='right'caption='[[1jdu]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1jdu]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_35091 Atcc 35091]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JDU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JDU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1jdu]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus Saccharolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JDU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JDU FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1jds|1jds]], [[1jdt|1jdt]], [[1jdv|1jdv]], [[1jdz|1jdz]], [[1je0|1je0]], [[1je1|1je1]]</div></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]] 2.5Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/S-methyl-5'-thioadenosine_phosphorylase S-methyl-5'-thioadenosine phosphorylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.28 2.4.2.28] </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=1jdu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jdu OCA], [https://pdbe.org/1jdu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jdu RCSB], [https://www.ebi.ac.uk/pdbsum/1jdu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jdu ProSAT]</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=1jdu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jdu OCA], [https://pdbe.org/1jdu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jdu RCSB], [https://www.ebi.ac.uk/pdbsum/1jdu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jdu ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/MTAP_SULSO MTAP_SULSO]] 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.<ref>PMID:15819883</ref>
| + | [https://www.uniprot.org/uniprot/PNPH_SACS2 PNPH_SACS2] Cleavage of guanosine or inosine to respective bases and sugar-1-phosphate molecules. Cleaves inosine, guanosine, and adenosine with a better efficiency than MTA.<ref>PMID:15819883</ref> <ref>PMID:7929153</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 35091]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: S-methyl-5'-thioadenosine phosphorylase]] | + | [[Category: Saccharolobus solfataricus]] |
| - | [[Category: Appleby, T C]] | + | [[Category: Appleby TC]] |
| - | [[Category: Cacciapuoti, G]] | + | [[Category: Cacciapuoti G]] |
| - | [[Category: Ealick, S E]] | + | [[Category: Ealick SE]] |
| - | [[Category: Mathews, I I]] | + | [[Category: Mathews II]] |
| - | [[Category: Porcelli, M]] | + | [[Category: Porcelli M]] |
| - | [[Category: Alpha-beta protein]]
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| - | [[Category: Transferase]]
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| Structural highlights
Function
PNPH_SACS2 Cleavage of guanosine or inosine to respective bases and sugar-1-phosphate molecules. Cleaves inosine, guanosine, and adenosine with a better efficiency than MTA.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The structure of 5'-deoxy-5'-methylthioadenosine phosphorylase from Sulfolobus solfataricus (SsMTAP) has been determined alone, as ternary complexes with sulfate plus substrates 5'-deoxy-5'-methylthioadenosine, adenosine, or guanosine, or with the noncleavable substrate analog Formycin B and as binary complexes with phosphate or sulfate alone. The structure of unliganded SsMTAP was refined at 2.5-A resolution and the structures of the complexes were refined at resolutions ranging from 1.6 to 2.0 A. SsMTAP is unusual both for its broad substrate specificity and for its extreme thermal stability. The hexameric structure of SsMTAP is similar to that of purine-nucleoside phosphorylase (PNP) from Escherichia coli, however, only SsMTAP accepts 5'-deoxy-5'-methylthioadenosine as a substrate. The active site of SsMTAP is similar to that of E. coli PNP with 13 of 18 nearest residues being identical. The main differences are at Thr(89), which corresponds to serine in E. coli PNP, and Glu(163), which corresponds to proline in E. coli PNP. In addition, a water molecule is found near the purine N-7 position in the guanosine complex of SsMTAP. Thr(89) is near the 5'-position of the nucleoside and may account for the ability of SsMTAP to accept either hydrophobic or hydrophilic substituents in that position. Unlike E. coli PNP, the structures of SsMTAP reveal a substrate-induced conformational change involving Glu(163). This residue is located at the interface between subunits and swings in toward the active site upon nucleoside binding. The high-resolution structures of SsMTAP suggest that the transition state is stabilized in different ways for 6-amino versus 6-oxo substrates. SsMTAP has optimal activity at 120 degrees C and retains full activity after 2 h at 100 degrees C. Examination of the three-dimensional structure of SsMTAP suggests that unlike most thermophilic enzymes, disulfide linkages play a key in role in its thermal stability.
Three-dimensional structure of a hyperthermophilic 5'-deoxy-5'-methylthioadenosine phosphorylase from Sulfolobus solfataricus.,Appleby TC, Mathews II, Porcelli M, Cacciapuoti G, Ealick SE J Biol Chem. 2001 Oct 19;276(42):39232-42. Epub 2001 Aug 6. PMID:11489901[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Cacciapuoti G, Forte S, Moretti MA, Brio A, Zappia V, Porcelli M. A novel hyperthermostable 5'-deoxy-5'-methylthioadenosine phosphorylase from the archaeon Sulfolobus solfataricus. FEBS J. 2005 Apr;272(8):1886-99. PMID:15819883 doi:http://dx.doi.org/10.1111/j.1742-4658.2005.04619.x
- ↑ Cacciapuoti G, Porcelli M, Bertoldo C, De Rosa M, Zappia V. Purification and characterization of extremely thermophilic and thermostable 5'-methylthioadenosine phosphorylase from the archaeon Sulfolobus solfataricus. Purine nucleoside phosphorylase activity and evidence for intersubunit disulfide bonds. J Biol Chem. 1994 Oct 7;269(40):24762-9 PMID:7929153
- ↑ Appleby TC, Mathews II, Porcelli M, Cacciapuoti G, Ealick SE. Three-dimensional structure of a hyperthermophilic 5'-deoxy-5'-methylthioadenosine phosphorylase from Sulfolobus solfataricus. J Biol Chem. 2001 Oct 19;276(42):39232-42. Epub 2001 Aug 6. PMID:11489901 doi:http://dx.doi.org/10.1074/jbc.M105694200
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