X-ray structure of imidazolonepropionase from Agrobacterium tumefaciens at 1.87 Å resolution
| Autor: | Rajiv Tyagi, Desigan Kumaran, Stephen K. Burley, Subramanyam Swaminathan |
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| Rok vydání: | 2007 |
| Předmět: |
Models
Molecular Binding Sites Amidohydrolase biology Protein Conformation Chemistry Stereochemistry Agrobacterium tumefaciens Crystallography X-Ray biology.organism_classification Biochemistry Catalysis Amidohydrolases Bacterial Proteins Structural Biology Hydrolase TIM barrel Enzyme kinetics Structural motif Molecular Biology Histidine Imidazolonepropionase |
| Zdroj: | Proteins: Structure, Function, and Bioinformatics. 69:652-658 |
| ISSN: | 0887-3585 |
| Popis: | Histidine degradation in Agrobacterium tumefaciens involves four enzymes, including histidase (EC 4.3.1.3), urocanase (EC 4.2.1.49), imidazolonepropionase (EC 3.5.2.7), and N-formylglutamate amidohydrolase (EC 3.5.3.8). The third enzyme of the pathway, imidazolone-propionase, a 45.6 kDa protein, catalyzes conversion of imidazolone-5-propanoate to N-forminio-L-glutamate. Initial studies of the role of imidazolonepropionase in histidine degradation were published in 1953. Subsequent publications have been limited to enzyme kinetics, crystallization, and a recently reported structure determination. The imidazolonepropionases are members of metallodepenent-hydrolases (or amidohydroase) superfamily, which includs ureases, adenosine deaminases, phosphotriesterases, dihydroorotases, allantoinases, hydantoinases, adenine and cytosine deaminases, imidazolonepropionases, aryldial-kylphosphatases, chlorohydrolases, and formylmethanofuran dehydroases. Proteins belonging to this large group share a common three-dimensional structural motif (an eightfold {alpha}/{beta} or TIM barrel) with similar active sites. Most superfamily members also share a conserved metal binding site, involving four histidine residues and one aspartic acid. Imidazolonepropionase is one of the targets selected for X-ray crystallpgrahpic structure determination by the New York Structural GenomiX Research Consortium (NYSGXRC) Target ID: 9252b to correlate the structure function relationship of poorly studied by important enzyme. Here they report the crystal structure of imidazolonepropionase from Agrobacterium tumefaciens determined at 1.87 {angstrom} resolution. |
| Databáze: | OpenAIRE |
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