3ftd: Difference between revisions

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{{Seed}}
[[Image:3ftd.jpg|left|200px]]


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==Crystal structure of A. aeolicus KsgA at 1.44-Angstrom resolution==
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<StructureSection load='3ftd' size='340' side='right'caption='[[3ftd]], [[Resolution|resolution]] 1.44&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[3ftd]] is a 1 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=3FTD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FTD FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.44&#8491;</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=3ftd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ftd OCA], [https://pdbe.org/3ftd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ftd RCSB], [https://www.ebi.ac.uk/pdbsum/3ftd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ftd ProSAT]</span></td></tr>
{{STRUCTURE_3ftd|  PDB=3ftd  |  SCENE=  }}
</table>
== 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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ft/3ftd_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3ftd ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.


===Crystal structure of A. aeolicus KsgA at 1.44-Angstrom resolution===
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<ref>PMID:19278652</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3ftd" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_19278652}}, adds the Publication Abstract to the page
*[[Adenosine dimethyltransferase 3D structures|Adenosine dimethyltransferase 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 19278652 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_19278652}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Aquifex aeolicus VF5]]
3FTD is a 1 chain structure of sequence from [http://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=3FTD OCA].
[[Category: Large Structures]]
 
[[Category: Ji X]]
==Reference==
[[Category: Tu C]]
<ref group="xtra">PMID:19278652</ref><references group="xtra"/>
[[Category: Aquifex aeolicus vf5]]
[[Category: Ji, X.]]
[[Category: Tu, C.]]
[[Category: Antibiotic resistance]]
[[Category: Ksga]]
[[Category: Methyltransferase]]
[[Category: Mtase]]
[[Category: Rna methyltransferase]]
[[Category: Rna-binding]]
[[Category: Rossmann-like fold]]
[[Category: Rrna processing]]
[[Category: S-adenosyl-l-methionine]]
[[Category: Transferase]]
 
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Retrieved from "https://proteopedia.org/3ftd"