1on3

<table><tr><td colspan='2'>[[1on3]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacterium_acidi_propionici_a"_von_freudenreich_and_orla-jensen_1907 "bacterium acidi propionici a" von freudenreich and orla-jensen 1907]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ON3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ON3 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=DXX:METHYLMALONIC+ACID'>DXX</scene>, <scene name='pdbligand=MCA:METHYLMALONYL-COENZYME+A'>MCA</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Methylmalonyl-CoA_carboxytransferase Methylmalonyl-CoA carboxytransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.3.1 2.1.3.1] </span></td></tr>

[[https://www.uniprot.org/uniprot/12S_PROFR 12S_PROFR]] The 12S subunit specifically catalyzes the transfer of the carboxyl group of methylmalonyl CoA to the biotin of the 1.3S subunit forming propanoyl-CoA and carboxylated 1.3S-biotin.

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== Publication Abstract from PubMed ==

Transcarboxylase from Propionibacterium shermanii is a 1.2 MDa multienzyme complex that couples two carboxylation reactions, transferring CO(2)(-) from methylmalonyl-CoA to pyruvate, yielding propionyl-CoA and oxaloacetate. The 1.9 A resolution crystal structure of the central 12S hexameric core, which catalyzes the first carboxylation reaction, has been solved bound to its substrate methylmalonyl-CoA. Overall, the structure reveals two stacked trimers related by 2-fold symmetry, and a domain duplication in the monomer. In the active site, the labile carboxylate group of methylmalonyl-CoA is stabilized by interaction with the N-termini of two alpha-helices. The 12S domains are structurally similar to the crotonase/isomerase superfamily, although only domain 1 of each 12S monomer binds ligand. The 12S reaction is similar to that of human propionyl-CoA carboxylase, whose beta-subunit has 50% sequence identity with 12S. A homology model of the propionyl-CoA carboxylase beta-subunit, based on this 12S crystal structure, provides new insight into the propionyl-CoA carboxylase mechanism, its oligomeric structure and the molecular basis of mutations responsible for enzyme deficiency in propionic acidemia.

Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core.,Hall PR, Wang YF, Rivera-Hainaj RE, Zheng X, Pustai-Carey M, Carey PR, Yee VC EMBO J. 2003 May 15;22(10):2334-47. PMID:12743028<ref>PMID:12743028</ref>

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

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== References ==

<references/>

[[Category: Bacterium acidi propionici a von freudenreich and orla-jensen 1907]]

[[Category: Methylmalonyl-CoA carboxytransferase]]

[[Category: Carey, P R]]

[[Category: Hall, P R]]

[[Category: Pustai-Carey, M]]

[[Category: Rivera-Hainaj, R E]]

[[Category: Wang, Y F]]

[[Category: Yee, V C]]

[[Category: Zheng, X]]

[[Category: Transferase]]