1tv2: Difference between revisions

Revision as of 08:57, 21 March 2018

Crystal structure of the hydroxylamine MtmB complex

Structural highlights

1tv2 is a 1 chain structure with sequence from Methanosarcina barkeri. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	BG5
Related:	1nth, 1l2q
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 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.

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

↑ Burke SA, Lo SL, Krzycki JA. Clustered genes encoding the methyltransferases of methanogenesis from monomethylamine. J Bacteriol. 1998 Jul;180(13):3432-40. PMID:9642198
↑ Burke SA, Krzycki JA. Reconstitution of Monomethylamine:Coenzyme M methyl transfer with a corrinoid protein and two methyltransferases purified from Methanosarcina barkeri. J Biol Chem. 1997 Jun 27;272(26):16570-7. PMID:9195968
↑ Hao B, Zhao G, Kang PT, Soares JA, Ferguson TK, Gallucci J, Krzycki JA, Chan MK. Reactivity and chemical synthesis of L-pyrrolysine- the 22(nd) genetically encoded amino acid. Chem Biol. 2004 Sep;11(9):1317-24. PMID:15380192 doi:10.1016/j.chembiol.2004.07.011

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OCA

[1] Burke SA, Lo SL, Krzycki JA. Clustered genes encoding the methyltransferases of methanogenesis from monomethylamine. J Bacteriol. 1998 Jul;180(13):3432-40. PMID:9642198

[2] Burke SA, Krzycki JA. Reconstitution of Monomethylamine:Coenzyme M methyl transfer with a corrinoid protein and two methyltransferases purified from Methanosarcina barkeri. J Biol Chem. 1997 Jun 27;272(26):16570-7. PMID:9195968

[3] Hao B, Zhao G, Kang PT, Soares JA, Ferguson TK, Gallucci J, Krzycki JA, Chan MK. Reactivity and chemical synthesis of L-pyrrolysine- the 22(nd) genetically encoded amino acid. Chem Biol. 2004 Sep;11(9):1317-24. PMID:15380192 doi:10.1016/j.chembiol.2004.07.011

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[2]

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@@ Line 1: / Line 1: @@
 ==Crystal structure of the hydroxylamine MtmB complex==
 <StructureSection load='1tv2' size='340' side='right' caption='[[1tv2]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BG5:5-HYDROXYAMINO-3-METHYL-PYRROLIDINE-2-CARBOXYLIC+ACID'>BG5</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tv2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tv2 OCA], [http://pdbe.org/1tv2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tv2 RCSB], [http://www.ebi.ac.uk/pdbsum/1tv2 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tv2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tv2 OCA], [http://pdbe.org/1tv2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tv2 RCSB], [http://www.ebi.ac.uk/pdbsum/1tv2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1tv2 ProSAT]</span></td></tr>
 </table>
 == Function ==

1tv2: Difference between revisions

Revision as of 08:57, 21 March 2018

Crystal structure of the hydroxylamine MtmB complex

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

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