1ksv: Difference between revisions
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<StructureSection load='1ksv' size='340' side='right'caption='[[1ksv]], [[Resolution|resolution]] 2.65Å' scene=''> | <StructureSection load='1ksv' size='340' side='right'caption='[[1ksv]], [[Resolution|resolution]] 2.65Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ksv]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1ksv]] 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=1KSV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KSV FirstGlance]. <br> | ||
</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> | </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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ksl|1ksl]], [[1ksk|1ksk]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ksl|1ksl]], [[1ksk|1ksk]]</div></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <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'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ksv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ksv OCA], [https://pdbe.org/1ksv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ksv RCSB], [https://www.ebi.ac.uk/pdbsum/1ksv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ksv ProSAT]</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> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
*[[Guide-independent Pseudouridine synthase|Guide-independent Pseudouridine synthase]] | *[[Guide-independent Pseudouridine synthase|Guide-independent Pseudouridine synthase]] | ||
*[[Pseudouridine synthase 3D structures|Pseudouridine synthase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 09:35, 18 August 2021
STRUCTURE OF RSUASTRUCTURE OF 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 PubMedIn 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 AlsoReferences
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