1f38

<table><tr><td colspan='2'>[[1f38]] 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=1F38 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1F38 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>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MT0146 ([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'>[http://proteopedia.org/fgij/fg.htm?mol=1f38 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f38 OCA], [http://pdbe.org/1f38 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1f38 RCSB], [http://www.ebi.ac.uk/pdbsum/1f38 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1f38 ProSAT], [http://www.topsan.org/Proteins/NESGC/1f38 TOPSAN]</span></td></tr>

[[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>

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== 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<ref>PMID:12429089</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1f38" style="background-color:#fffaf0;"></div>

[[Category: Hunt, J F]]

[[Category: Keller, J P]]

[[Category: Structural genomic]]

[[Category: Smith, P M]]

[[Category: PSI, Protein structure initiative]]