3ftf: Difference between revisions
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<StructureSection load='3ftf' size='340' side='right'caption='[[3ftf]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='3ftf' size='340' side='right'caption='[[3ftf]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3ftf]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3ftf]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus_VF5 Aquifex aeolicus VF5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FTF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FTF FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></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=3ftf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ftf OCA], [https://pdbe.org/3ftf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ftf RCSB], [https://www.ebi.ac.uk/pdbsum/3ftf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ftf 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=3ftf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ftf OCA], [https://pdbe.org/3ftf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ftf RCSB], [https://www.ebi.ac.uk/pdbsum/3ftf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ftf ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/RSMA_AQUAE RSMA_AQUAE] Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits (By similarity). | |||
== 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: | [[Category: Aquifex aeolicus VF5]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Ji | [[Category: Ji X]] | ||
[[Category: Tu | [[Category: Tu C]] | ||
Latest revision as of 16:08, 30 August 2023
Crystal structure of A. aeolicus KsgA in complex with RNA and SAHCrystal structure of A. aeolicus KsgA in complex with RNA and SAH
Structural highlights
FunctionRSMA_AQUAE Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits (By similarity). 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 PubMedAmong methyltransferases, KsgA and the reaction it catalyzes are conserved throughout evolution. However, the specifics of substrate recognition by the enzyme remain unknown. Here we report structures of Aquifex aeolicus KsgA, in its ligand-free form, in complex with RNA, and in complex with both RNA and S-adenosylhomocysteine (SAH, reaction product of cofactor S-adenosylmethionine), revealing critical structural information on KsgA-RNA and KsgA-SAH interactions. Moreover, the structures show how conformational changes that occur upon RNA binding create the cofactor-binding site. There are nine conserved functional motifs (motifs I-VIII and X) in KsgA. Prior to RNA binding, motifs I and VIII are flexible, each exhibiting two distinct conformations. Upon RNA binding, the two motifs become stabilized in one of these conformations, which is compatible with the binding of SAH. Motif X, which is also stabilized upon RNA binding, is directly involved in the binding of SAH. Structural basis for binding of RNA and cofactor by a KsgA methyltransferase.,Tu C, Tropea JE, Austin BP, Court DL, Waugh DS, Ji X Structure. 2009 Mar 11;17(3):374-85. PMID:19278652[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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