1dd2: Difference between revisions

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[[Image:1dd2.gif|left|200px]]<br /><applet load="1dd2" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1dd2.gif|left|200px]]<br /><applet load="1dd2" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1dd2" />

'''BIOTIN CARBOXYL CARRIER DOMAIN OF TRANSCARBOXYLASE (TC 1.3S)'''<br />

==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.

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 [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Propionibacterium_freudenreichii_subsp._shermanii Propionibacterium freudenreichii subsp. shermanii]. Active as [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] Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1DD2 OCA].

1DD2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Propionibacterium_freudenreichii_subsp._shermanii Propionibacterium freudenreichii subsp. shermanii]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DD2 OCA].

==Reference==

Line 14:

[[Category: Propionibacterium freudenreichii subsp. shermanii]]

[[Category: Single protein]]

[[Category: Carey, P.R.]]

[[Category: Carey, P R.]]

[[Category: Reddy, D.V.]]

[[Category: Reddy, D V.]]

[[Category: Shenoy, B.C.]]

[[Category: Shenoy, B C.]]

[[Category: Sonnichsen, F.D.]]

[[Category: Sonnichsen, F D.]]

[[Category: antiparallel beta sheet]]

[[Category: biocytin]]

[[Category: hammerhead]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:15:24 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1dd2.gif|left|200px]]<br /><applet load="1dd2" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1dd2.gif|left|200px]]<br /><applet load="1dd2" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1dd2" />
 '''BIOTIN CARBOXYL CARRIER DOMAIN OF TRANSCARBOXYLASE (TC 1.3S)'''<br />
 ==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.
+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==
-DD2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Propionibacterium_freudenreichii_subsp._shermanii Propionibacterium freudenreichii subsp. shermanii]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DD2 OCA].
+DD2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Propionibacterium_freudenreichii_subsp._shermanii Propionibacterium freudenreichii subsp. shermanii]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DD2 OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Propionibacterium freudenreichii subsp. shermanii]]
 [[Category: Single protein]]
-[[Category: Carey, P.R.]]
+[[Category: Carey, P R.]]
-[[Category: Reddy, D.V.]]
+[[Category: Reddy, D V.]]
-[[Category: Shenoy, B.C.]]
+[[Category: Shenoy, B C.]]
-[[Category: Sonnichsen, F.D.]]
+[[Category: Sonnichsen, F D.]]
 [[Category: antiparallel beta sheet]]
 [[Category: biocytin]]
 [[Category: hammerhead]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:10:59 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:15:24 2008''