1dd2

<StructureSection load='1dd2' size='340' side='right'caption='[[1dd2]], [[NMR_Ensembles_of_Models | 32 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1dd2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"propionibacterium_shermanii"_van_niel_1928 "propionibacterium shermanii" van niel 1928]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DD2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DD2 FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1dcz|1dcz]]</div></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/BCCP_PROFR BCCP_PROFR]] The biotinyl 1.3S subunit serves as a carboxyl carrier between the substrate-binding sites on the 12S and 5S subunits.

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== Publication Abstract from PubMed ==

Transcarboxylase (TC) from Propionibacterium shermanii, a biotin-dependent enzyme, catalyzes the transfer of a carboxyl group from methylmalonyl-CoA to pyruvate to form propionyl-CoA and oxalacetate. Within the multi-subunit enzyme complex, the 1.3S subunit functions as the carboxyl group carrier and also binds the other two subunits to assist in the overall assembly of the enzyme. The 1.3S subunit is a 123 amino acid polypeptide (12.6 kDa) to which biotin is covalently attached at Lys 89. The three-dimensional solution structure of the full-length holo-1.3S subunit of TC has been solved by multidimensional heteronuclear NMR spectroscopy. The C-terminal half of the protein (51-123) is folded into a compact all-beta-domain comprising of two four-stranded antiparallel beta-sheets connected by short loops and turns. The fold exhibits a high 2-fold internal symmetry and is similar to that of the biotin carboxyl carrier protein (BCCP) of acetyl-CoA carboxylase, but lacks an extension that has been termed "protruding thumb" in BCCP. The first 50 residues, which have been shown to be involved in intersubunit interactions in the intact enzyme, appear to be disordered in the isolated 1.3S subunit. The molecular surface of the folded domain has two distinct surfaces: one side is highly charged, while the other comprises mainly hydrophobic, highly conserved residues.

High resolution solution structure of the 1.3S subunit of transcarboxylase from Propionibacterium shermanii.,Reddy DV, Shenoy BC, Carey PR, Sonnichsen FD Biochemistry. 2000 Mar 14;39(10):2509-16. PMID:10704200<ref>PMID:10704200</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 1dd2" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Propionibacterium shermanii van niel 1928]]

[[Category: Methylmalonyl-CoA carboxytransferase]]

[[Category: Carey, P R]]

[[Category: Reddy, D V]]

[[Category: Shenoy, B C]]

[[Category: Sonnichsen, F D]]

[[Category: Transferase]]