1dd2

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[[Image:1dd2.gif|left|200px]]
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{{Structure
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|PDB= 1dd2 |SIZE=350|CAPTION= <scene name='initialview01'>1dd2</scene>
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The line below this paragraph, containing "STRUCTURE_1dd2", creates the "Structure Box" on the page.
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Methylmalonyl-CoA_carboxytransferase Methylmalonyl-CoA carboxytransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.3.1 2.1.3.1] </span>
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{{STRUCTURE_1dd2| PDB=1dd2 | SCENE= }}
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|RELATEDENTRY=[[1dcz|1DCZ]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dd2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dd2 OCA], [http://www.ebi.ac.uk/pdbsum/1dd2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dd2 RCSB]</span>
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'''BIOTIN CARBOXYL CARRIER DOMAIN OF TRANSCARBOXYLASE (TC 1.3S)'''
'''BIOTIN CARBOXYL CARRIER DOMAIN OF TRANSCARBOXYLASE (TC 1.3S)'''
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[[Category: Shenoy, B C.]]
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[[Category: antiparallel beta sheet]]
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[[Category: biocytin]]
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Revision as of 10:42, 2 May 2008

Image:1dd2.gif

Template:STRUCTURE 1dd2

BIOTIN CARBOXYL CARRIER DOMAIN OF TRANSCARBOXYLASE (TC 1.3S)


Overview

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.

About this Structure

1DD2 is a Single protein structure of sequence from Propionibacterium freudenreichii subsp. shermanii. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Fri May 2 13:42:44 2008

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