1pkv
From Proteopedia
(New page: 200px<br /><applet load="1pkv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pkv, resolution 2.60Å" /> '''The N-terminal domai...) |
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| - | [[Image:1pkv.jpg|left|200px]]<br /><applet load="1pkv" size=" | + | [[Image:1pkv.jpg|left|200px]]<br /><applet load="1pkv" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1pkv, resolution 2.60Å" /> | caption="1pkv, resolution 2.60Å" /> | ||
'''The N-terminal domain of riboflavin synthase in complex with riboflavin'''<br /> | '''The N-terminal domain of riboflavin synthase in complex with riboflavin'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Riboflavin synthase of Escherichia coli is a homotrimer with a molecular | + | Riboflavin synthase of Escherichia coli is a homotrimer with a molecular mass of 70 kDa. The enzyme catalyzes the dismutation of 6,7-dimethyl-8-(1'-D-ribityl)-lumazine, affording riboflavin and 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione. The N-terminal segment (residues 1-87) and the C-terminal segment (residues 98-187) form beta-barrels with similar fold and a high degree of sequence similarity. A recombinant peptide comprising amino acid residues 1-97 forms a dimer, which binds riboflavin with high affinity. Here, we report the structure of this construct in complex with riboflavin at 2.6A resolution. It is demonstrated that the complex can serve as a model for ligand-binding in the native enzyme. The structure and riboflavin-binding mode is in excellent agreement with structural information obtained from the native enzyme from Escherichia coli and riboflavin synthase from Schizosaccharomyces pombe. The implications for the binding specificity and the regiospecificity of the catalyzed reaction are discussed. |
==About this Structure== | ==About this Structure== | ||
| - | 1PKV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with RBF as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Riboflavin_synthase Riboflavin synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.9 2.5.1.9] Full crystallographic information is available from [http:// | + | 1PKV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=RBF:'>RBF</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Riboflavin_synthase Riboflavin synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.9 2.5.1.9] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PKV OCA]. |
==Reference== | ==Reference== | ||
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[[Category: greek key motif]] | [[Category: greek key motif]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:29:54 2008'' |
Revision as of 12:29, 21 February 2008
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The N-terminal domain of riboflavin synthase in complex with riboflavin
Overview
Riboflavin synthase of Escherichia coli is a homotrimer with a molecular mass of 70 kDa. The enzyme catalyzes the dismutation of 6,7-dimethyl-8-(1'-D-ribityl)-lumazine, affording riboflavin and 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione. The N-terminal segment (residues 1-87) and the C-terminal segment (residues 98-187) form beta-barrels with similar fold and a high degree of sequence similarity. A recombinant peptide comprising amino acid residues 1-97 forms a dimer, which binds riboflavin with high affinity. Here, we report the structure of this construct in complex with riboflavin at 2.6A resolution. It is demonstrated that the complex can serve as a model for ligand-binding in the native enzyme. The structure and riboflavin-binding mode is in excellent agreement with structural information obtained from the native enzyme from Escherichia coli and riboflavin synthase from Schizosaccharomyces pombe. The implications for the binding specificity and the regiospecificity of the catalyzed reaction are discussed.
About this Structure
1PKV is a Single protein structure of sequence from Escherichia coli with as ligand. Active as Riboflavin synthase, with EC number 2.5.1.9 Full crystallographic information is available from OCA.
Reference
The structure of the N-terminal domain of riboflavin synthase in complex with riboflavin at 2.6A resolution., Meining W, Eberhardt S, Bacher A, Ladenstein R, J Mol Biol. 2003 Aug 29;331(5):1053-63. PMID:12927541
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