1lab

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[[Image:1lab.jpg|left|200px]]
[[Image:1lab.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1lab |SIZE=350|CAPTION= <scene name='initialview01'>1lab</scene>
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The line below this paragraph, containing "STRUCTURE_1lab", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND=
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= BACILLUS STEAROTHERMOPHILUS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1422 Geobacillus stearothermophilus])
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|DOMAIN=
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{{STRUCTURE_1lab| PDB=1lab | SCENE= }}
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|RELATEDENTRY=[[1lac|1LAC]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lab OCA], [http://www.ebi.ac.uk/pdbsum/1lab PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lab RCSB]</span>
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}}
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'''THREE-DIMENSIONAL STRUCTURE OF THE LIPOYL DOMAIN FROM BACILLUS STEAROTHERMOPHILUS PYRUVATE DEHYDROGENASE MULTIENZYME COMPLEX'''
'''THREE-DIMENSIONAL STRUCTURE OF THE LIPOYL DOMAIN FROM BACILLUS STEAROTHERMOPHILUS PYRUVATE DEHYDROGENASE MULTIENZYME COMPLEX'''
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[[Category: Laue, E D.]]
[[Category: Laue, E D.]]
[[Category: Perham, R N.]]
[[Category: Perham, R N.]]
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[[Category: transferase (acyltransferase)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:43:25 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:00:21 2008''
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Revision as of 20:43, 2 May 2008

Template:STRUCTURE 1lab

THREE-DIMENSIONAL STRUCTURE OF THE LIPOYL DOMAIN FROM BACILLUS STEAROTHERMOPHILUS PYRUVATE DEHYDROGENASE MULTIENZYME COMPLEX


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.

About this Structure

1LAB is a Single protein structure of sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA.

Reference

Three-dimensional structure of the lipoyl domain from Bacillus stearothermophilus pyruvate dehydrogenase multienzyme complex., Dardel F, Davis AL, Laue ED, Perham RN, J Mol Biol. 1993 Feb 20;229(4):1037-48. PMID:8445635 Page seeded by OCA on Fri May 2 23:43:25 2008

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