1M33
Crystal Structure of BioH at 1.7 A
Summary for 1M33
| Entry DOI | 10.2210/pdb1m33/pdb |
| Descriptor | BioH protein, 3-HYDROXY-PROPANOIC ACID, 1,2-ETHANEDIOL, ... (4 entities in total) |
| Functional Keywords | alpha-betta-alpha sandwich, structural genomics, psi, protein structure initiative, midwest center for structural genomics, mcsg, unknown function |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 29186.70 |
| Authors | Sanishvili, R.,Savchenko, A.,Skarina, T.,Edwards, A.,Joachimiak, A.,Yakunin, A.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2002-06-26, release date: 2003-01-21, Last modification date: 2019-07-24) |
| Primary citation | Sanishvili, R.,Yakunin, A.F.,Laskowski, R.A.,Skarina, T.,Evdokimova, E.,Doherty-Kirby, A.,Lajoie, G.A.,Thornton, J.M.,Arrowsmith, C.H.,Savchenko, A.,Joachimiak, A.,Edwards, A.M. Integrating structure, bioinformatics, and enzymology to discover function: BioH, a new carboxylesterase from Escherichia coli. J.Biol.Chem., 278:26039-26045, 2003 Cited by PubMed Abstract: Structural proteomics projects are generating three-dimensional structures of novel, uncharacterized proteins at an increasing rate. However, structure alone is often insufficient to deduce the specific biochemical function of a protein. Here we determined the function for a protein using a strategy that integrates structural and bioinformatics data with parallel experimental screening for enzymatic activity. BioH is involved in biotin biosynthesis in Escherichia coli and had no previously known biochemical function. The crystal structure of BioH was determined at 1.7 A resolution. An automated procedure was used to compare the structure of BioH with structural templates from a variety of different enzyme active sites. This screen identified a catalytic triad (Ser82, His235, and Asp207) with a configuration similar to that of the catalytic triad of hydrolases. Analysis of BioH with a panel of hydrolase assays revealed a carboxylesterase activity with a preference for short acyl chain substrates. The combined use of structural bioinformatics with experimental screens for detecting enzyme activity could greatly enhance the rate at which function is determined from structure. PubMed: 12732651DOI: 10.1074/jbc.M303867200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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