7dcy: Difference between revisions

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<StructureSection load='7dcy' size='340' side='right'caption='[[7dcy]], [[Resolution|resolution]] 1.97&Aring;' scene=''>
<StructureSection load='7dcy' size='340' side='right'caption='[[7dcy]], [[Resolution|resolution]] 1.97&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7dcy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycge Mycge]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DCY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DCY FirstGlance]. <br>
<table><tr><td colspan='2'>[[7dcy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycoplasma_genitalium_G37 Mycoplasma genitalium G37]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DCY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DCY FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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]] 1.972&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rnr, vacB, MG104 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243273 MYCGE])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Exoribonuclease_II Exoribonuclease II], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.13.1 3.1.13.1] </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=7dcy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dcy OCA], [https://pdbe.org/7dcy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dcy RCSB], [https://www.ebi.ac.uk/pdbsum/7dcy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dcy 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=7dcy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dcy OCA], [https://pdbe.org/7dcy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dcy RCSB], [https://www.ebi.ac.uk/pdbsum/7dcy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dcy ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/RNR_MYCGE RNR_MYCGE]] 3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs.  
[https://www.uniprot.org/uniprot/RNR_MYCGE RNR_MYCGE] 3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 7dcy" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 7dcy" style="background-color:#fffaf0;"></div>
==See Also==
*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Exoribonuclease II]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Mycge]]
[[Category: Mycoplasma genitalium G37]]
[[Category: Abula, A]]
[[Category: Abula A]]
[[Category: Chen, Q]]
[[Category: Chen Q]]
[[Category: Ji, X]]
[[Category: Ji X]]
[[Category: Li, T]]
[[Category: Li T]]
[[Category: Li, X]]
[[Category: Li X]]
[[Category: Quan, X]]
[[Category: Quan X]]
[[Category: Yang, T]]
[[Category: Yang T]]
[[Category: Hydrolase]]
[[Category: Rna 2'-o-methylation sensitive]]
[[Category: Rna hydrolase]]

Latest revision as of 19:30, 29 November 2023

Apo form of Mycoplasma genitalium RNase RApo form of Mycoplasma genitalium RNase R

Structural highlights

7dcy is a 1 chain structure with sequence from Mycoplasma genitalium G37. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.972Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RNR_MYCGE 3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs.

Publication Abstract from PubMed

RNA 2'-O-methylation is widely distributed and plays important roles in various cellular processes. Mycoplasma genitalium RNase R (MgR), a prokaryotic member of the RNase II/RNB family, is a 3'-5' exoribonuclease and is particularly sensitive to RNA 2'-O-methylation. However, how RNase R interacts with various RNA species and exhibits remarkable sensitivity to substrate 2'-O-methyl modifications remains elusive. Here we report high-resolution crystal structures of MgR in apo form and in complex with various RNA substrates. The structural data together with extensive biochemical analysis quantitively illustrate MgR's ribonuclease activity and significant sensitivity to RNA 2'-O-methylation. Comparison to its related homologs reveals an exquisite mechanism for the recognition and degradation of RNA substrates. Through structural and mutagenesis studies, we identified proline 277 to be responsible for the significant sensitivity of MgR to RNA 2'-O-methylation within the RNase II/RNB family. We also generated several MgR variants with modulated activities. Our work provides a mechanistic understanding of MgR activity that can be harnessed as a powerful RNA analytical tool that will open up a new venue for RNA 2'-O-methylations research in biological and clinical samples.

Molecular mechanism of RNase R substrate sensitivity for RNA ribose methylation.,Abula A, Li X, Quan X, Yang T, Liu Y, Guo H, Li T, Ji X Nucleic Acids Res. 2021 Mar 31. pii: 6206732. doi: 10.1093/nar/gkab202. PMID:33788943[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Abula A, Li X, Quan X, Yang T, Liu Y, Guo H, Li T, Ji X. Molecular mechanism of RNase R substrate sensitivity for RNA ribose methylation. Nucleic Acids Res. 2021 Mar 31. pii: 6206732. doi: 10.1093/nar/gkab202. PMID:33788943 doi:http://dx.doi.org/10.1093/nar/gkab202

7dcy, resolution 1.97Å

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OCA