8x46: Difference between revisions
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==Crystal structure of DIMT1 in complex with adenosylornithine (SFG) from Pyrococcus horikoshii== | |||
<StructureSection load='8x46' size='340' side='right'caption='[[8x46]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8x46]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii_OT3 Pyrococcus horikoshii OT3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8X46 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8X46 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</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=8x46 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8x46 OCA], [https://pdbe.org/8x46 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8x46 RCSB], [https://www.ebi.ac.uk/pdbsum/8x46 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8x46 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/RSMA_PYRHO RSMA_PYRHO] Specifically dimethylates two adjacent adenosines 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.[HAMAP-Rule:MF_00607] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Dimethyladenosine transferase 1 (DIMT1), an ortholog of bacterial KsgA is a conserved protein that assists in ribosome biogenesis by modifying two successive adenosine bases near the 3' end of small subunit (SSU) rRNA. Although KsgA/DIMT1 proteins have been characterized in bacteria and eukaryotes, they are yet unexplored in archaea. Also, their dynamics are not well understood. Here, we structurally and functionally characterized the apo and holo forms of archaeal DIMT1 from Pyrococcus horikoshii. Wild-type protein and mutants were analyzed to capture different transition states, including open, closed, and intermediate states. This study reports a unique inter-domain movement that is needed for substrate (RNA) positioning in the catalytic pocket, and is only observed in the presence of the cognate cofactors S-adenosyl-L-methionine (SAM) or S-adenosyl-L-homocysteine (SAH). The binding of the inhibitor sinefungine, an analog of SAM or SAH, to archaeal DIMT1 blocks the catalytic pocket and renders the enzyme inactive. | |||
Structural and functional characterization of archaeal DIMT1 unveils distinct protein dynamics essential for efficient catalysis.,Saha S, Kanaujia SP Structure. 2024 Aug 2:S0969-2126(24)00276-4. doi: 10.1016/j.str.2024.07.013. PMID:39146930<ref>PMID:39146930</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 8x46" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Pyrococcus horikoshii OT3]] | |||
[[Category: Kanaujia SP]] | |||
[[Category: Saha S]] | |||
Latest revision as of 08:24, 28 August 2024
Crystal structure of DIMT1 in complex with adenosylornithine (SFG) from Pyrococcus horikoshiiCrystal structure of DIMT1 in complex with adenosylornithine (SFG) from Pyrococcus horikoshii
Structural highlights
FunctionRSMA_PYRHO Specifically dimethylates two adjacent adenosines 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.[HAMAP-Rule:MF_00607] Publication Abstract from PubMedDimethyladenosine transferase 1 (DIMT1), an ortholog of bacterial KsgA is a conserved protein that assists in ribosome biogenesis by modifying two successive adenosine bases near the 3' end of small subunit (SSU) rRNA. Although KsgA/DIMT1 proteins have been characterized in bacteria and eukaryotes, they are yet unexplored in archaea. Also, their dynamics are not well understood. Here, we structurally and functionally characterized the apo and holo forms of archaeal DIMT1 from Pyrococcus horikoshii. Wild-type protein and mutants were analyzed to capture different transition states, including open, closed, and intermediate states. This study reports a unique inter-domain movement that is needed for substrate (RNA) positioning in the catalytic pocket, and is only observed in the presence of the cognate cofactors S-adenosyl-L-methionine (SAM) or S-adenosyl-L-homocysteine (SAH). The binding of the inhibitor sinefungine, an analog of SAM or SAH, to archaeal DIMT1 blocks the catalytic pocket and renders the enzyme inactive. Structural and functional characterization of archaeal DIMT1 unveils distinct protein dynamics essential for efficient catalysis.,Saha S, Kanaujia SP Structure. 2024 Aug 2:S0969-2126(24)00276-4. doi: 10.1016/j.str.2024.07.013. PMID:39146930[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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