4qnx
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4qnx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QNX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QNX FirstGlance]. <br> | <table><tr><td colspan='2'>[[4qnx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QNX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QNX FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.619Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4qnx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qnx OCA], [https://pdbe.org/4qnx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qnx RCSB], [https://www.ebi.ac.uk/pdbsum/4qnx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qnx 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=4qnx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qnx OCA], [https://pdbe.org/4qnx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qnx RCSB], [https://www.ebi.ac.uk/pdbsum/4qnx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qnx ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/CMOB_ECOLI CMOB_ECOLI] Catalyzes the conversion of 5-hydroxyuridine (ho5U) to 5-methoxyuridine (mo5U) at position 34 in tRNA.[HAMAP-Rule:MF_01590] | [https://www.uniprot.org/uniprot/CMOB_ECOLI CMOB_ECOLI] Catalyzes the conversion of 5-hydroxyuridine (ho5U) to 5-methoxyuridine (mo5U) at position 34 in tRNA.[HAMAP-Rule:MF_01590] | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Enzyme-mediated modifications at the wobble position of tRNAs are essential for the translation of the genetic code. We report the genetic, biochemical and structural characterization of CmoB, the enzyme that recognizes the unique metabolite carboxy-S-adenosine-L-methionine (Cx-SAM) and catalyzes a carboxymethyl transfer reaction resulting in formation of 5-oxyacetyluridine at the wobble position of tRNAs. CmoB is distinctive in that it is the only known member of the SAM-dependent methyltransferase (SDMT) superfamily that utilizes a naturally occurring SAM analog as the alkyl donor to fulfill a biologically meaningful function. Biochemical and genetic studies define the in vitro and in vivo selectivity for Cx-SAM as alkyl donor over the vastly more abundant SAM. Complementary high-resolution structures of the apo- and Cx-SAM bound CmoB reveal the determinants responsible for this remarkable discrimination. Together, these studies provide mechanistic insight into the enzymatic and non-enzymatic feature of this alkyl transfer reaction which affords the broadened specificity required for tRNAs to recognize multiple synonymous codons. | ||
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| - | Determinants of the CmoB carboxymethyl transferase utilized for selective tRNA wobble modification.,Kim J, Xiao H, Koh J, Wang Y, Bonanno JB, Thomas K, Babbitt PC, Brown S, Lee YS, Almo SC Nucleic Acids Res. 2015 Apr 8. pii: gkv206. PMID:25855808<ref>PMID:25855808</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4qnx" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[TRNA methyltransferase 3D structures|TRNA methyltransferase 3D structures]] | *[[TRNA methyltransferase 3D structures|TRNA methyltransferase 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Crystal structure of apo-CmoB
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