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| | <StructureSection load='1ksl' size='340' side='right'caption='[[1ksl]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='1ksl' size='340' side='right'caption='[[1ksl]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1ksl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KSL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KSL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1ksl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KSL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KSL FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=URA:URACIL'>URA</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]] 2.1Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=URA:URACIL'>URA</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ksk|1ksk]], [[1ksv|1ksv]]</div></td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Pseudouridylate_synthase Pseudouridylate synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.70 4.2.1.70] </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=1ksl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ksl OCA], [https://pdbe.org/1ksl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ksl RCSB], [https://www.ebi.ac.uk/pdbsum/1ksl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ksl ProSAT], [https://www.topsan.org/Proteins/BSGI/1ksl TOPSAN]</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=1ksl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ksl OCA], [https://pdbe.org/1ksl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ksl RCSB], [https://www.ebi.ac.uk/pdbsum/1ksl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ksl ProSAT], [https://www.topsan.org/Proteins/BSGI/1ksl TOPSAN]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/RSUA_ECOLI RSUA_ECOLI]] Responsible for synthesis of pseudouridine from uracil-516 in 16S ribosomal RNA.<ref>PMID:7612632</ref> <ref>PMID:10376875</ref>
| + | [https://www.uniprot.org/uniprot/RSUA_ECOLI RSUA_ECOLI] Responsible for synthesis of pseudouridine from uracil-516 in 16S ribosomal RNA.<ref>PMID:7612632</ref> <ref>PMID:10376875</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: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pseudouridylate synthase]]
| + | [[Category: Cygler M]] |
| - | [[Category: Structural genomic]]
| + | [[Category: Larocque R]] |
| - | [[Category: Cygler, M]] | + | [[Category: Matte A]] |
| - | [[Category: Larocque, R]] | + | [[Category: Sauve V]] |
| - | [[Category: Matte, A]] | + | [[Category: Schrag JD]] |
| - | [[Category: Sauve, V]] | + | [[Category: Sivaraman J]] |
| - | [[Category: Schrag, J D]] | + | [[Category: Stura EA]] |
| - | [[Category: Sivaraman, J]] | + | |
| - | [[Category: Stura, E A]] | + | |
| - | [[Category: Bsgi]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Pseudouridine synthase]]
| + | |
| - | [[Category: Rsua]]
| + | |
| Structural highlights
Function
RSUA_ECOLI Responsible for synthesis of pseudouridine from uracil-516 in 16S ribosomal RNA.[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
In Escherichia coli, the pseudouridine synthase RsuA catalyzes formation of pseudouridine (psi) at position 516 in 16S rRNA during assembly of the 30S ribosomal subunit. We have determined the crystal structure of RsuA bound to uracil at 2.0 A resolution and to uridine 5'-monophosphate (UMP) at 2.65 A resolution. RsuA consists of an N-terminal domain connected by an extended linker to the central and C-terminal domains. Uracil and UMP bind in a cleft between the central and C-terminal domains near the catalytic residue Asp 102. The N-terminal domain shows structural similarity to the ribosomal protein S4. Despite only 15% amino acid identity, the other two domains are structurally similar to those of the tRNA-specific psi-synthase TruA, including the position of the catalytic Asp. Our results suggest that all four families of pseudouridine synthases share the same fold of their catalytic domain(s) and uracil-binding site.
Structure of the 16S rRNA pseudouridine synthase RsuA bound to uracil and UMP.,Sivaraman J, Sauve V, Larocque R, Stura EA, Schrag JD, Cygler M, Matte A Nat Struct Biol. 2002 May;9(5):353-8. PMID:11953756[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Wrzesinski J, Bakin A, Nurse K, Lane BG, Ofengand J. Purification, cloning, and properties of the 16S RNA pseudouridine 516 synthase from Escherichia coli. Biochemistry. 1995 Jul 11;34(27):8904-13. PMID:7612632
- ↑ Conrad J, Niu L, Rudd K, Lane BG, Ofengand J. 16S ribosomal RNA pseudouridine synthase RsuA of Escherichia coli: deletion, mutation of the conserved Asp102 residue, and sequence comparison among all other pseudouridine synthases. RNA. 1999 Jun;5(6):751-63. PMID:10376875
- ↑ Sivaraman J, Sauve V, Larocque R, Stura EA, Schrag JD, Cygler M, Matte A. Structure of the 16S rRNA pseudouridine synthase RsuA bound to uracil and UMP. Nat Struct Biol. 2002 May;9(5):353-8. PMID:11953756 doi:10.1038/nsb788
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