1bbl: Difference between revisions

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THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE E3-BINDING DOMAIN OF THE DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE CORE FROM THE 2-OXOGLUTARATE DEHYDROGENASE MULTIENZYME COMPLEX OF ESCHERICHIA COLI

OverviewOverview

The three-dimensional solution structure of a 51-residue synthetic peptide comprising the dihydrolipoamide dehydrogenase (E3)-binding domain of the dihydrolipoamide succinyltransferase (E2) core of the 2-oxoglutarate dehydrogenase multienzyme complex of Escherichia coli has been determined by nuclear magnetic resonance spectroscopy and hybrid distance geometry-dynamical simulated annealing calculations. The structure is based on 630 approximate interproton distance and 101 torsion angle (phi, psi, chi 1) restraints. A total of 56 simulated annealing structures were calculated, and the atomic rms distribution about the mean coordinate positions for residues 12-48 of the synthetic peptide is 1.24 A for the backbone atoms, 1.68 A for all atoms, and 1.33 A for all atoms excluding the six side chains which are disordered at chi 1 and the seven which are disordered at chi 2; when the irregular partially disordered loop from residues 31 to 39 is excluded, the rms distribution drops to 0.77 A for the backbone atoms, 1.55 A for all atoms, and 0.89 A for ordered side chains. Although proton resonance assignments for the N-terminal 11 residues and the C-terminal 3 residues were obtained, these two segments of the polypeptide are disordered in solution as evidenced by the absence of nonsequential nuclear Overhauser effects. The solution structure of the E3-binding domain consists of two parallel helices (residues 14-23 and 40-48), a short extended strand (24-26), a five-residue helical-like turn, and an irregular (and more disordered) loop (residues 31-39). This report presents the first structure of an E3-binding domain from a 2-oxo acid dehydrogenase complex.(ABSTRACT TRUNCATED AT 250 WORDS)

About this StructureAbout this Structure

1BBL is a Single protein structure of sequence from Escherichia coli. Active as Dihydrolipoyllysine-residue succinyltransferase, with EC number 2.3.1.61 Full crystallographic information is available from OCA.

ReferenceReference

Three-dimensional solution structure of the E3-binding domain of the dihydrolipoamide succinyltransferase core from the 2-oxoglutarate dehydrogenase multienzyme complex of Escherichia coli., Robien MA, Clore GM, Omichinski JG, Perham RN, Appella E, Sakaguchi K, Gronenborn AM, Biochemistry. 1992 Apr 7;31(13):3463-71. PMID:1554728

Page seeded by OCA on Thu Feb 21 11:53:32 2008

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OCA

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-[[Image:1bbl.gif|left|200px]]<br /><applet load="1bbl" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1bbl.gif|left|200px]]<br /><applet load="1bbl" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1bbl" />
 '''THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE E3-BINDING DOMAIN OF THE DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE CORE FROM THE 2-OXOGLUTARATE DEHYDROGENASE MULTIENZYME COMPLEX OF ESCHERICHIA COLI'''<br />
 ==Overview==
-The three-dimensional solution structure of a 51-residue synthetic peptide, comprising the dihydrolipoamide dehydrogenase (E3)-binding domain of the, dihydrolipoamide succinyltransferase (E2) core of the 2-oxoglutarate, dehydrogenase multienzyme complex of Escherichia coli has been determined, by nuclear magnetic resonance spectroscopy and hybrid distance, geometry-dynamical simulated annealing calculations. The structure is, based on 630 approximate interproton distance and 101 torsion angle (phi, psi, chi 1) restraints. A total of 56 simulated annealing structures were, calculated, and the atomic rms distribution about the mean coordinate, positions for residues 12-48 of the synthetic peptide is 1.24 A for the, backbone atoms, 1.68 A for all atoms, and 1.33 A for all atoms excluding, the six side chains which are disordered at chi 1 and the seven which are, disordered at chi 2; when the irregular partially disordered loop from, residues 31 to 39 is excluded, the rms distribution drops to 0.77 A for, the backbone atoms, 1.55 A for all atoms, and 0.89 A for ordered side, chains. Although proton resonance assignments for the N-terminal 11, residues and the C-terminal 3 residues were obtained, these two segments, of the polypeptide are disordered in solution as evidenced by the absence, of nonsequential nuclear Overhauser effects. The solution structure of the, E3-binding domain consists of two parallel helices (residues 14-23 and, 40-48), a short extended strand (24-26), a five-residue helical-like turn, and an irregular (and more disordered) loop (residues 31-39). This report, presents the first structure of an E3-binding domain from a 2-oxo acid, dehydrogenase complex.(ABSTRACT TRUNCATED AT 250 WORDS)
+The three-dimensional solution structure of a 51-residue synthetic peptide comprising the dihydrolipoamide dehydrogenase (E3)-binding domain of the dihydrolipoamide succinyltransferase (E2) core of the 2-oxoglutarate dehydrogenase multienzyme complex of Escherichia coli has been determined by nuclear magnetic resonance spectroscopy and hybrid distance geometry-dynamical simulated annealing calculations. The structure is based on 630 approximate interproton distance and 101 torsion angle (phi, psi, chi 1) restraints. A total of 56 simulated annealing structures were calculated, and the atomic rms distribution about the mean coordinate positions for residues 12-48 of the synthetic peptide is 1.24 A for the backbone atoms, 1.68 A for all atoms, and 1.33 A for all atoms excluding the six side chains which are disordered at chi 1 and the seven which are disordered at chi 2; when the irregular partially disordered loop from residues 31 to 39 is excluded, the rms distribution drops to 0.77 A for the backbone atoms, 1.55 A for all atoms, and 0.89 A for ordered side chains. Although proton resonance assignments for the N-terminal 11 residues and the C-terminal 3 residues were obtained, these two segments of the polypeptide are disordered in solution as evidenced by the absence of nonsequential nuclear Overhauser effects. The solution structure of the E3-binding domain consists of two parallel helices (residues 14-23 and 40-48), a short extended strand (24-26), a five-residue helical-like turn, and an irregular (and more disordered) loop (residues 31-39). This report presents the first structure of an E3-binding domain from a 2-oxo acid dehydrogenase complex.(ABSTRACT TRUNCATED AT 250 WORDS)
 ==About this Structure==
-BBL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Dihydrolipoyllysine-residue_succinyltransferase Dihydrolipoyllysine-residue succinyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.61 2.3.1.61] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BBL OCA].
+BBL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Dihydrolipoyllysine-residue_succinyltransferase Dihydrolipoyllysine-residue succinyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.61 2.3.1.61] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BBL OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Escherichia coli]]
 [[Category: Single protein]]
-[[Category: Clore, G.M.]]
+[[Category: Clore, G M.]]
-[[Category: Gronenborn, A.M.]]
+[[Category: Gronenborn, A M.]]
-[[Category: Robien, M.A.]]
+[[Category: Robien, M A.]]
 [[Category: glycolysis]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:31:33 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:53:32 2008''