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3vse

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Current revision (08:41, 20 March 2024) (edit) (undo)
 
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<StructureSection load='3vse' size='340' side='right'caption='[[3vse]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='3vse' size='340' side='right'caption='[[3vse]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3vse]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Staam Staam]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VSE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VSE FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3vse]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_Mu50 Staphylococcus aureus subsp. aureus Mu50]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VSE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VSE FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.099&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2b78|2b78]], [[3ldf|3ldf]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SAV1081 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=158878 STAAM])</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=3vse FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vse OCA], [https://pdbe.org/3vse PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vse RCSB], [https://www.ebi.ac.uk/pdbsum/3vse PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vse 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=3vse FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vse OCA], [https://pdbe.org/3vse PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vse RCSB], [https://www.ebi.ac.uk/pdbsum/3vse PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vse ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/A0A0H3JYW8_STAAM A0A0H3JYW8_STAAM]
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Cluster of Orthologous Groups (COG) 1092 contains two distinct types of methylation enzyme from Escherichia coli, YccW and YcbY. YccW is a 5-methylcytosine methyltransferase (m5C MTase) responsible for m5C 1962 in 23S rRNA, whereas YcbY is a dimethyltransferase, of which N- and C-terminal domains are responsible for N2- methylguanosine (m2G) 2445 and 7-methylguanosine (m7G) 2069 in 23S rRNA, respectively. However, proteins in COG1092 other than YccW and YcbY remain functionally unidentified. SAV1081 from Staphylococcus aureus is one of the functionally unassigned proteins of COG1092. Although SAV1081 has an identical domain organization to YccW with 26% sequence identity, it lacks the catalytic cysteine residue essential for m5C formation activity. In the present study, we determined the crystal structure of SAV1081 and compared it with those of other COG1092 proteins. Based on the structure characteristics, such as the presence or absence of the catalytic cysteine residue, beta-hairpin structure, and oligomeric state, as well as domain organization, we propose a functional classification of COG1092 proteins.
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Crystal Structure of a Putative Methyltransferase SAV1081 from Staphylococcus aureus.,Kita S, Tanaka Y, Hirano N, Kimura S, Suzuki T, Suzuki T, Yao M, Tanaka I Protein Pept Lett. 2013 May 1;20(5):530-7. PMID:23016631<ref>PMID:23016631</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3vse" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Staam]]
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[[Category: Staphylococcus aureus subsp. aureus Mu50]]
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[[Category: Kita, S]]
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[[Category: Kita S]]
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[[Category: Tanaka, I]]
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[[Category: Tanaka I]]
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[[Category: Tanaka, Y]]
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[[Category: Tanaka Y]]
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[[Category: Yao, M]]
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[[Category: Yao M]]
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[[Category: Methyltransferase]]
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[[Category: Rossmann fold]]
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[[Category: Transferase]]
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Current revision

Crystal structure of methyltransferase

PDB ID 3vse

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