1tv3: Difference between revisions
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<StructureSection load='1tv3' size='340' side='right'caption='[[1tv3]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='1tv3' size='340' side='right'caption='[[1tv3]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1tv3]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1tv3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanosarcina_barkeri Methanosarcina barkeri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TV3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TV3 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BG4:5-(HYDROXY-METHYL-AMINO)-3-METHYL-PYRROLIDINE-2-CARBOXYLIC+ACID'>BG4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BG4:5-(HYDROXY-METHYL-AMINO)-3-METHYL-PYRROLIDINE-2-CARBOXYLIC+ACID'>BG4</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1nth|1nth]], [[1l2q|1l2q]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1nth|1nth]], [[1l2q|1l2q]]</div></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1tv3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tv3 OCA], [https://pdbe.org/1tv3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tv3 RCSB], [https://www.ebi.ac.uk/pdbsum/1tv3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tv3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/MTMB1_METBA MTMB1_METBA]] Catalyzes the transfer of the methyl group from monomethylamine to the corrinoid cofactor of MtmC (MtmC1 or MtmC2).<ref>PMID:9642198</ref> <ref>PMID:9195968</ref> | ||
<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 1tv3" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1tv3" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 12:33, 29 September 2021
Crystal structure of the N-methyl-hydroxylamine MtmB complexCrystal structure of the N-methyl-hydroxylamine MtmB complex
Structural highlights
Function[MTMB1_METBA] Catalyzes the transfer of the methyl group from monomethylamine to the corrinoid cofactor of MtmC (MtmC1 or MtmC2).[1] [2] Publication Abstract from PubMedL-pyrrolysine, the 22(nd) genetically encoded amino acid, was previously deduced to be (4R, 5R)-4-substituted-pyrroline-5-carboxylate attached to the epsilon-nitrogen of lysine based on the crystal structure of the M. barkeri monomethylamine methyltransferase (MtmB). To confirm L-pyrrolysine's identity, structures of MtmB have been determined following treatment with hydroxylamine, N-methylhydroxylamine, or dithionite. Analysis of these structures has provided additional support for the presence of the pyrroline ring and, together with previous mass spectroscopy data, has led us to assign the C(4)-substituent to a methyl group. Based on this assignment, synthetic L-pyrrolysine was prepared by chemical methods. Detailed study of this chemically synthesized L-pyrrolysine has allowed us to characterize its physical properties, to study its chemical stability, and to elucidate the role of its C(4) substituent. Future applications of this synthetic L-pyrrolysine include its in vivo incorporation into recombinant proteins. Reactivity and chemical synthesis of L-pyrrolysine- the 22(nd) genetically encoded amino acid.,Hao B, Zhao G, Kang PT, Soares JA, Ferguson TK, Gallucci J, Krzycki JA, Chan MK Chem Biol. 2004 Sep;11(9):1317-24. PMID:15380192[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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