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| | <StructureSection load='1gxb' size='340' side='right'caption='[[1gxb]], [[Resolution|resolution]] 2.65Å' scene=''> | | <StructureSection load='1gxb' size='340' side='right'caption='[[1gxb]], [[Resolution|resolution]] 2.65Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1gxb]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GXB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GXB FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1gxb]] is a 4 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=1GXB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GXB FirstGlance]. <br> |
| - | </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>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</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]] 2.65Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1o17|1o17]]</div></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>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Anthranilate_phosphoribosyltransferase Anthranilate phosphoribosyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.18 2.4.2.18] </span></td></tr>
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| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gxb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gxb OCA], [https://pdbe.org/1gxb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gxb RCSB], [https://www.ebi.ac.uk/pdbsum/1gxb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gxb 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=1gxb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gxb OCA], [https://pdbe.org/1gxb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gxb RCSB], [https://www.ebi.ac.uk/pdbsum/1gxb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gxb ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/TRPD_SULSO TRPD_SULSO]] Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).<ref>PMID:11298741</ref> <ref>PMID:16714288</ref>
| + | [https://www.uniprot.org/uniprot/TRPD_SACS2 TRPD_SACS2] Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).[HAMAP-Rule:MF_00211]<ref>PMID:11298741</ref> <ref>PMID:16714288</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: Anthranilate phosphoribosyltransferase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Sulfolobus solfataricus]] | + | [[Category: Saccharolobus solfataricus]] |
| - | [[Category: Ivens, A]] | + | [[Category: Ivens A]] |
| - | [[Category: Kirschner, K]] | + | [[Category: Kirschner K]] |
| - | [[Category: Mayans, O]] | + | [[Category: Mayans O]] |
| - | [[Category: Nissen, L J]] | + | [[Category: Nissen LJ]] |
| - | [[Category: Wilmanns, M]] | + | [[Category: Wilmanns M]] |
| - | [[Category: Anthranilate phosphoribosyl transferase]]
| + | |
| - | [[Category: Mg2+]]
| + | |
| - | [[Category: Prpp]]
| + | |
| - | [[Category: Pyrophosphate]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Tryptophane biosynthesis]]
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| Structural highlights
Function
TRPD_SACS2 Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).[HAMAP-Rule:MF_00211][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 crystal structure of the dimeric anthranilate phosphoribosyltransferase (AnPRT) reveals a new category of phosphoribosyltransferases, designated as class III. The active site of this enzyme is located within the flexible hinge region of its two-domain structure. The pyrophosphate moiety of phosphoribosylpyrophosphate is co-ordinated by a metal ion and is bound by two conserved loop regions within this hinge region. With the structure of AnPRT available, structural analysis of all enzymatic activities of the tryptophan biosynthesis pathway is complete, thereby connecting the evolution of its enzyme members to the general development of metabolic processes. Its structure reveals it to have the same fold, topology, active site location and type of association as class II nucleoside phosphorylases. At the level of sequences, this relationship is mirrored by 13 structurally invariant residues common to both enzyme families. Taken together, these data imply common ancestry of enzymes catalysing reverse biological processes--the ribosylation and deribosylation of metabolic pathway intermediates. These relationships establish new links for enzymes involved in nucleotide and amino acid metabolism.
Structural analysis of two enzymes catalysing reverse metabolic reactions implies common ancestry.,Mayans O, Ivens A, Nissen LJ, Kirschner K, Wilmanns M EMBO J. 2002 Jul 1;21(13):3245-54. PMID:12093726[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ivens A, Mayans O, Szadkowski H, Wilmanns M, Kirschner K. Purification, characterization and crystallization of thermostable anthranilate phosphoribosyltransferase from Sulfolobus solfataricus. Eur J Biochem. 2001 Apr;268(8):2246-52. PMID:11298741
- ↑ Marino M, Deuss M, Svergun DI, Konarev PV, Sterner R, Mayans O. Structural and mutational analysis of substrate complexation by anthranilate phosphoribosyltransferase from Sulfolobus solfataricus. J Biol Chem. 2006 Jul 28;281(30):21410-21. Epub 2006 May 19. PMID:16714288 doi:10.1074/jbc.M601403200
- ↑ Mayans O, Ivens A, Nissen LJ, Kirschner K, Wilmanns M. Structural analysis of two enzymes catalysing reverse metabolic reactions implies common ancestry. EMBO J. 2002 Jul 1;21(13):3245-54. PMID:12093726 doi:http://dx.doi.org/10.1093/emboj/cdf298
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