1lab: Difference between revisions

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

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

caption="1lab" />

'''THREE-DIMENSIONAL STRUCTURE OF THE LIPOYL DOMAIN FROM BACILLUS STEAROTHERMOPHILUS PYRUVATE DEHYDROGENASE MULTIENZYME COMPLEX'''<br />

==Overview==

The structure of the lipoyl domain from the pyruvate dehydrogenase, multienzyme complex of Bacillus stearothermophilus has been determined by, means of nuclear magnetic resonance spectroscopy. A total of 452 nuclear, Overhauser effect distance constraints and 76 dihedral angle restraints, were employed as the input for the structure calculations, which were, performed using a hybrid distance geometry-simulated annealing strategy, and the programs DISGEO and X-PLOR. The overall structure of the lipoyl, domain (residues 1 to 79 of the dihydrolipoamide acetyltransferase, polypeptide chain) is that of a flattened eight-stranded beta-barrel, folded around a core of well-defined hydrophobic residues. The lipoylation, site, lysine 42, is located in the middle of a beta-turn, and the N and, C-terminal residues of the domain are close together in adjacent, beta-strands at the opposite end of the molecule. The polypeptide backbone, exhibits a 2-fold axis of quasi-symmetry, with the C alpha atoms of, residues 15 to 39 and 52 to 76 being almost superimposable on those of, residues 52 to 76 and 15 to 39, respectively (root-mean-square deviation =, 1.48 A). The amino acid residues at key positions in the structure are, conserved among all the reported primary structures of lipoyl domains, suggesting that the domains all fold in a similar way.

The structure of the lipoyl domain from the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus has been determined by means of nuclear magnetic resonance spectroscopy. A total of 452 nuclear Overhauser effect distance constraints and 76 dihedral angle restraints were employed as the input for the structure calculations, which were performed using a hybrid distance geometry-simulated annealing strategy and the programs DISGEO and X-PLOR. The overall structure of the lipoyl domain (residues 1 to 79 of the dihydrolipoamide acetyltransferase polypeptide chain) is that of a flattened eight-stranded beta-barrel folded around a core of well-defined hydrophobic residues. The lipoylation site, lysine 42, is located in the middle of a beta-turn, and the N and C-terminal residues of the domain are close together in adjacent beta-strands at the opposite end of the molecule. The polypeptide backbone exhibits a 2-fold axis of quasi-symmetry, with the C alpha atoms of residues 15 to 39 and 52 to 76 being almost superimposable on those of residues 52 to 76 and 15 to 39, respectively (root-mean-square deviation = 1.48 A). The amino acid residues at key positions in the structure are conserved among all the reported primary structures of lipoyl domains, suggesting that the domains all fold in a similar way.

==About this Structure==

1LAB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Active as [http://en.wikipedia.org/wiki/Dihydrolipoyllysine-residue_acetyltransferase Dihydrolipoyllysine-residue acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.12 2.3.1.12] Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1LAB OCA].

1LAB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Active as [http://en.wikipedia.org/wiki/Dihydrolipoyllysine-residue_acetyltransferase Dihydrolipoyllysine-residue acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.12 2.3.1.12] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LAB OCA].

==Reference==

Line 15:

[[Category: Single protein]]

[[Category: Dardel, F.]]

[[Category: Davis, A.L.]]

[[Category: Davis, A L.]]

[[Category: Laue, E.D.]]

[[Category: Laue, E D.]]

[[Category: Perham, R.N.]]

[[Category: Perham, R N.]]

[[Category: transferase (acyltransferase)]]

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@@ Line 1: / Line 1: @@
-[[Image:1lab.jpg|left|200px]]<br /><applet load="1lab" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1lab.jpg|left|200px]]<br /><applet load="1lab" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1lab" />
 '''THREE-DIMENSIONAL STRUCTURE OF THE LIPOYL DOMAIN FROM BACILLUS STEAROTHERMOPHILUS PYRUVATE DEHYDROGENASE MULTIENZYME COMPLEX'''<br />
 ==Overview==
-The structure of the lipoyl domain from the pyruvate dehydrogenase, multienzyme complex of Bacillus stearothermophilus has been determined by, means of nuclear magnetic resonance spectroscopy. A total of 452 nuclear, Overhauser effect distance constraints and 76 dihedral angle restraints, were employed as the input for the structure calculations, which were, performed using a hybrid distance geometry-simulated annealing strategy, and the programs DISGEO and X-PLOR. The overall structure of the lipoyl, domain (residues 1 to 79 of the dihydrolipoamide acetyltransferase, polypeptide chain) is that of a flattened eight-stranded beta-barrel, folded around a core of well-defined hydrophobic residues. The lipoylation, site, lysine 42, is located in the middle of a beta-turn, and the N and, C-terminal residues of the domain are close together in adjacent, beta-strands at the opposite end of the molecule. The polypeptide backbone, exhibits a 2-fold axis of quasi-symmetry, with the C alpha atoms of, residues 15 to 39 and 52 to 76 being almost superimposable on those of, residues 52 to 76 and 15 to 39, respectively (root-mean-square deviation =, 1.48 A). The amino acid residues at key positions in the structure are, conserved among all the reported primary structures of lipoyl domains, suggesting that the domains all fold in a similar way.
+The structure of the lipoyl domain from the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus has been determined by means of nuclear magnetic resonance spectroscopy. A total of 452 nuclear Overhauser effect distance constraints and 76 dihedral angle restraints were employed as the input for the structure calculations, which were performed using a hybrid distance geometry-simulated annealing strategy and the programs DISGEO and X-PLOR. The overall structure of the lipoyl domain (residues 1 to 79 of the dihydrolipoamide acetyltransferase polypeptide chain) is that of a flattened eight-stranded beta-barrel folded around a core of well-defined hydrophobic residues. The lipoylation site, lysine 42, is located in the middle of a beta-turn, and the N and C-terminal residues of the domain are close together in adjacent beta-strands at the opposite end of the molecule. The polypeptide backbone exhibits a 2-fold axis of quasi-symmetry, with the C alpha atoms of residues 15 to 39 and 52 to 76 being almost superimposable on those of residues 52 to 76 and 15 to 39, respectively (root-mean-square deviation = 1.48 A). The amino acid residues at key positions in the structure are conserved among all the reported primary structures of lipoyl domains, suggesting that the domains all fold in a similar way.
 ==About this Structure==
-LAB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Active as [http://en.wikipedia.org/wiki/Dihydrolipoyllysine-residue_acetyltransferase Dihydrolipoyllysine-residue acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.12 2.3.1.12] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LAB OCA].
+LAB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Active as [http://en.wikipedia.org/wiki/Dihydrolipoyllysine-residue_acetyltransferase Dihydrolipoyllysine-residue acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.12 2.3.1.12] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LAB OCA].
 ==Reference==
@@ Line 15: / Line 15: @@
 [[Category: Single protein]]
 [[Category: Dardel, F.]]
-[[Category: Davis, A.L.]]
+[[Category: Davis, A L.]]
-[[Category: Laue, E.D.]]
+[[Category: Laue, E D.]]
-[[Category: Perham, R.N.]]
+[[Category: Perham, R N.]]
 [[Category: transferase (acyltransferase)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:25:23 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:43:03 2008''