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| | <StructureSection load='1l3c' size='340' side='right'caption='[[1l3c]], [[Resolution|resolution]] 2.31Å' scene=''> | | <StructureSection load='1l3c' size='340' side='right'caption='[[1l3c]], [[Resolution|resolution]] 2.31Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1l3c]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"methanobacterium_thermoautotrophicus"_(sic)_zeikus_and_wolfe_1972 "methanobacterium thermoautotrophicus" (sic) zeikus and wolfe 1972]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L3C OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1L3C FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1l3c]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L3C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L3C FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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]] 2.31Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1kxz|1kxz]], [[1f38|1f38]], [[1l3b|1l3b]], [[1l3i|1l3i]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Mth146 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=145262 "Methanobacterium thermoautotrophicus" (sic) Zeikus and Wolfe 1972])</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=1l3c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l3c OCA], [https://pdbe.org/1l3c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l3c RCSB], [https://www.ebi.ac.uk/pdbsum/1l3c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l3c ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1l3c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l3c OCA], [http://pdbe.org/1l3c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1l3c RCSB], [http://www.ebi.ac.uk/pdbsum/1l3c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1l3c ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CBIT_METTH CBIT_METTH]] Catalyzes the methylation of C-15 in cobalt-precorrin-6B followed by the decarboxylation of C-12 to form cobalt-precorrin-7 (Probable).<ref>PMID:12429089</ref> | + | [https://www.uniprot.org/uniprot/CBIT_METTH CBIT_METTH] Catalyzes the methylation of C-15 in cobalt-precorrin-6B followed by the decarboxylation of C-12 to form cobalt-precorrin-7 (Probable).<ref>PMID:12429089</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Benach, J]] | + | [[Category: Methanothermobacter thermautotrophicus]] |
| - | [[Category: Christendat, D]] | + | [[Category: Benach J]] |
| - | [[Category: Hunt, J F]] | + | [[Category: Christendat D]] |
| - | [[Category: Keller, J P]] | + | [[Category: Hunt JF]] |
| - | [[Category: Smith, P M]] | + | [[Category: Keller JP]] |
| - | [[Category: DeTitta, G]] | + | [[Category: Smith PM]] |
| - | [[Category: Beta barrel]]
| + | [[Category: DeTitta G]] |
| - | [[Category: Decarboxylase]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Methyltransferase]]
| + | |
| - | [[Category: Rossmann fold]]
| + | |
| - | [[Category: Structural genomic]]
| + | |
| - | [[Category: Structure-based function assignment]]
| + | |
| - | [[Category: Tetramer]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
CBIT_METTH Catalyzes the methylation of C-15 in cobalt-precorrin-6B followed by the decarboxylation of C-12 to form cobalt-precorrin-7 (Probable).[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The CbiT and CbiE enzymes participate in the biosynthesis of vitamin B12. They are fused together in some organisms to form a protein called CobL, which catalyzes two methylations and one decarboxylation on a precorrin intermediate. Because CbiE has sequence homology to canonical precorrin methyltransferases, CbiT was hypothesized to catalyze the decarboxylation. We herein present the crystal structure of MT0146, the CbiT homolog from Methanobacterium thermoautotrophicum. The protein shows structural similarity to Rossmann-like S-adenosyl-methionine-dependent methyltransferases, and our 1.9 A cocrystal structure shows that it binds S-adenosyl-methionine in standard geometry near a binding pocket that could accommodate a precorrin substrate. Therefore, MT0146/CbiT probably functions as a precorrin methyltransferase and represents the first enzyme identified with this activity that does not have the canonical precorrin methyltransferase fold.
The crystal structure of MT0146/CbiT suggests that the putative precorrin-8w decarboxylase is a methyltransferase.,Keller JP, Smith PM, Benach J, Christendat D, deTitta GT, Hunt JF Structure. 2002 Nov;10(11):1475-87. PMID:12429089[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Keller JP, Smith PM, Benach J, Christendat D, deTitta GT, Hunt JF. The crystal structure of MT0146/CbiT suggests that the putative precorrin-8w decarboxylase is a methyltransferase. Structure. 2002 Nov;10(11):1475-87. PMID:12429089
- ↑ Keller JP, Smith PM, Benach J, Christendat D, deTitta GT, Hunt JF. The crystal structure of MT0146/CbiT suggests that the putative precorrin-8w decarboxylase is a methyltransferase. Structure. 2002 Nov;10(11):1475-87. PMID:12429089
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