7v2m: Difference between revisions
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==== | ==T.thermophilus 30S ribosome with KsgA, class K1k4== | ||
<StructureSection load='7v2m' size='340' side='right'caption='[[7v2m]]' scene=''> | <StructureSection load='7v2m' size='340' side='right'caption='[[7v2m]], [[Resolution|resolution]] 3.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | <table><tr><td colspan='2'>[[7v2m]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7V2M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7V2M FirstGlance]. <br> | ||
</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=7v2m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7v2m OCA], [https://pdbe.org/7v2m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7v2m RCSB], [https://www.ebi.ac.uk/pdbsum/7v2m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7v2m ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.4Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=7v2m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7v2m OCA], [https://pdbe.org/7v2m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7v2m RCSB], [https://www.ebi.ac.uk/pdbsum/7v2m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7v2m ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/RS2_THET8 RS2_THET8] Spans the head-body hinge region of the 30S subunit. Is loosely associated with the 30S subunit.[HAMAP-Rule:MF_00291_B] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Methylation of specific nucleotides is integral for ribosomal biogenesis and also serves as a common mechanism to confer antibiotic resistance by pathogenic bacteria. Here, by determining the high-resolution structure of the 30S-KsgA complex by cryo-electron microscopy, a state was captured, where KsgA juxtaposes between helices h44 and h45 of the 30S ribosome, separating them, thereby enabling remodeling of the surrounded rRNA and allowing the cognate site to enter the methylation pocket. With the structure as a guide, several mutant versions of the ribosomes, where interacting bases in the catalytic helix h45 and surrounding helices h44, h24, and h27, were mutated and evaluated for their methylation efficiency revealing factors that direct the enzyme to its cognate site with high fidelity. The biochemical studies show that the three-dimensional environment of the ribosome enables the interaction of select loop regions in KsgA with the ribosome helices paramount to maintain selectivity. | |||
Decoding the Mechanism of Specific RNA Targeting by Ribosomal Methyltransferases.,Singh J, Raina R, Vinothkumar KR, Anand R ACS Chem Biol. 2022 Apr 15;17(4):829-839. doi: 10.1021/acschembio.1c00732. Epub , 2022 Mar 22. PMID:35316014<ref>PMID:35316014</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7v2m" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Adenosine dimethyltransferase 3D structures|Adenosine dimethyltransferase 3D structures]] | |||
*[[Ribosomal protein THX 3D structures|Ribosomal protein THX 3D structures]] | |||
*[[Ribosome 3D structures|Ribosome 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Thermus thermophilus HB8]] | ||
[[Category: Anand R]] | |||
[[Category: Raina R]] | |||
[[Category: Singh J]] | |||
[[Category: Vinothkumar KR]] | |||
Latest revision as of 08:15, 12 June 2024
T.thermophilus 30S ribosome with KsgA, class K1k4T.thermophilus 30S ribosome with KsgA, class K1k4
Structural highlights
FunctionRS2_THET8 Spans the head-body hinge region of the 30S subunit. Is loosely associated with the 30S subunit.[HAMAP-Rule:MF_00291_B] Publication Abstract from PubMedMethylation of specific nucleotides is integral for ribosomal biogenesis and also serves as a common mechanism to confer antibiotic resistance by pathogenic bacteria. Here, by determining the high-resolution structure of the 30S-KsgA complex by cryo-electron microscopy, a state was captured, where KsgA juxtaposes between helices h44 and h45 of the 30S ribosome, separating them, thereby enabling remodeling of the surrounded rRNA and allowing the cognate site to enter the methylation pocket. With the structure as a guide, several mutant versions of the ribosomes, where interacting bases in the catalytic helix h45 and surrounding helices h44, h24, and h27, were mutated and evaluated for their methylation efficiency revealing factors that direct the enzyme to its cognate site with high fidelity. The biochemical studies show that the three-dimensional environment of the ribosome enables the interaction of select loop regions in KsgA with the ribosome helices paramount to maintain selectivity. Decoding the Mechanism of Specific RNA Targeting by Ribosomal Methyltransferases.,Singh J, Raina R, Vinothkumar KR, Anand R ACS Chem Biol. 2022 Apr 15;17(4):829-839. doi: 10.1021/acschembio.1c00732. Epub , 2022 Mar 22. PMID:35316014[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also
References
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