1cbf

<table><tr><td colspan='2'>[[1cbf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_14581 Atcc 14581]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CBF OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1CBF FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CBIF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1404 ATCC 14581])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Precorrin-4_C(11)-methyltransferase Precorrin-4 C(11)-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.133 2.1.1.133] </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=1cbf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cbf OCA], [http://pdbe.org/1cbf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1cbf RCSB], [http://www.ebi.ac.uk/pdbsum/1cbf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1cbf ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/CBIF_BACME CBIF_BACME]] Catalyzes the methylation of C-11 in cobalt-precorrin-4 to form cobalt-precorrin-5A.

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== Publication Abstract from PubMed ==

Biosynthesis of the corrin ring of vitamin B12 requires the action of six S-adenosyl-L-methionine (AdoMet) dependent transmethylases, closely related in sequence. The first X-ray structure of one of these, cobalt-precorrin-4 transmethylase, CbiF, from Bacillus megaterium has been determined to a resolution of 2.4 A. CbiF contains two alphabeta domains forming a trough in which S-adenosyl-L-homocysteine (AdoHcy) binds. The location of AdoHcy and a number of conserved residues, helps define the precorrin binding site. A second crystal form determined at 3.1 A resolution highlights the flexibility of two loops around this site. CbiF employs a unique mode of AdoHcy binding and represents a new class of transmethylase.

The X-ray structure of a cobalamin biosynthetic enzyme, cobalt-precorrin-4 methyltransferase.,Schubert HL, Wilson KS, Raux E, Woodcock SC, Warren MJ Nat Struct Biol. 1998 Jul;5(7):585-92. PMID:9665173<ref>PMID:9665173</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 1cbf" style="background-color:#fffaf0;"></div>

[[Category: Atcc 14581]]

[[Category: Raux, E]]

[[Category: Schubert, H L]]

[[Category: Warren, M J]]

[[Category: Wilson, K S]]

[[Category: Woodcock, S C]]

[[Category: Cobalamin biosynthesis]]

[[Category: Precorrin-4 methyltransferase]]