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| | <StructureSection load='3fte' size='340' side='right'caption='[[3fte]], [[Resolution|resolution]] 3.00Å' scene=''> | | <StructureSection load='3fte' size='340' side='right'caption='[[3fte]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3fte]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquae Aquae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FTE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FTE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3fte]] 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=3FTE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FTE 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;'>[[1qyr|1qyr]], [[1zq9|1zq9]], [[1g38|1g38]], [[3ftc|3ftc]], [[3ftd|3ftd]], [[3ftf|3ftf]]</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]] 3Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aq_1816, ksgA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224324 AQUAE])</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=3fte FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fte OCA], [https://pdbe.org/3fte PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fte RCSB], [https://www.ebi.ac.uk/pdbsum/3fte PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fte 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=3fte FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fte OCA], [https://pdbe.org/3fte PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fte RCSB], [https://www.ebi.ac.uk/pdbsum/3fte PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fte 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).
| + | [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: Aquae]] | + | [[Category: Aquifex aeolicus VF5]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ji, X]] | + | [[Category: Ji X]] |
| - | [[Category: Tu, C]] | + | [[Category: Tu C]] |
| - | [[Category: Antibiotic resistance]]
| + | |
| - | [[Category: Ksga]]
| + | |
| - | [[Category: Methyltransferase]]
| + | |
| - | [[Category: Mtase]]
| + | |
| - | [[Category: Rna]]
| + | |
| - | [[Category: Rna methyltransferase]]
| + | |
| - | [[Category: Rna-binding]]
| + | |
| - | [[Category: Rossmann-like fold]]
| + | |
| - | [[Category: Rrna processing]]
| + | |
| - | [[Category: S-adenosyl-l-methionine]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Transferase-rna complex]]
| + | |
| Structural highlights
Function
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
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Among 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 Also
References
- ↑ Tu C, Tropea JE, Austin BP, Court DL, Waugh DS, Ji X. Structural basis for binding of RNA and cofactor by a KsgA methyltransferase. Structure. 2009 Mar 11;17(3):374-85. PMID:19278652 doi:10.1016/j.str.2009.01.010
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