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== | ==Crystal structure of the N-methyl-hydroxylamine MtmB complex== | ||
<StructureSection load='1tv3' size='340' side='right'caption='[[1tv3]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<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='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='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='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> | |||
== 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;"> | |||
== Publication Abstract from PubMed == | |||
L-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. | L-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<ref>PMID:15380192</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1tv3" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Methanosarcina barkeri]] | [[Category: Methanosarcina barkeri]] | ||
[[Category: Chan MK]] | |||
[[Category: Chan | [[Category: Ferguson TK]] | ||
[[Category: Ferguson | [[Category: Gallucci J]] | ||
[[Category: Gallucci | [[Category: Hao B]] | ||
[[Category: Hao | [[Category: Kang PT]] | ||
[[Category: Kang | [[Category: Krzycki JA]] | ||
[[Category: Krzycki | [[Category: Soares JA]] | ||
[[Category: Soares | [[Category: Zhao G]] | ||
[[Category: Zhao | |||
Latest revision as of 09:04, 5 July 2023
Crystal structure of the N-methyl-hydroxylamine MtmB complexCrystal structure of the N-methyl-hydroxylamine MtmB complex
Structural highlights
FunctionMTMB1_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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