Crystal structures of a subunit of the formylglycinamide ribonucleotide amidotransferase, PurS, fromThermus thermophilus,Sulfolobus tokodaiiandMethanocaldococcus jannaschii
| Autor: | Lirong Chen, Yuzo Watanabe, Gota Kawai, Bi-Cheng Wang, Zheng-Qing Fu, Akio Ebihara, Sakiko Suzuki, Hisaaki Yanai, Ryoji Masui, Satoko Tamura, Kiyoshi Okada, Seiki Kuramitsu, Shigeyuki Yokoyama, Mayumi Kanagawa, John Chrzas, Seiki Baba, Yoshihiro Agari, Takashi Kumasaka, Noriko Nakagawa, Gen Ichi Sampei |
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| Rok vydání: | 2016 |
| Předmět: |
Models
Molecular Protein Conformation alpha-Helical 0301 basic medicine Stereochemistry Archaeal Proteins Dimer Protein subunit Biophysics Sulfolobus tokodaii Gene Expression Crystal structure Molecular Dynamics Simulation Crystallography X-Ray Biochemistry Sulfolobus Research Communications 03 medical and health sciences chemistry.chemical_compound Bacterial Proteins Structural Biology Escherichia coli Genetics Protein Interaction Domains and Motifs Amino Acid Sequence Cloning Molecular Glutamine amidotransferase Binding Sites Sequence Homology Amino Acid 030102 biochemistry & molecular biology biology Chemistry Thermus thermophilus Methanocaldococcus jannaschii Condensed Matter Physics biology.organism_classification Formylglycinamide ribonucleotide Recombinant Proteins Protein Structure Tertiary Protein Subunits Methanocaldococcus Protein Conformation beta-Strand Carbon-Nitrogen Ligases with Glutamine as Amide-N-Donor Protein Multimerization Sequence Alignment Plasmids Protein Binding |
| Zdroj: | Acta Crystallographica Section F Structural Biology Communications. 72:627-635 |
| ISSN: | 2053-230X |
| DOI: | 10.1107/s2053230x1600978x |
| Popis: | The crystal structures of a subunit of the formylglycinamide ribonucleotide amidotransferase, PurS, fromThermus thermophilus,Sulfolobus tokodaiiandMethanocaldococcus jannaschiiwere determined and their structural characteristics were analyzed. For PurS fromT. thermophilus, two structures were determined using two crystals that were grown in different conditions. The four structures in the dimeric form were almost identical to one another despite their relatively low sequence identities. This is also true for all PurS structures determined to date. A few residues were conserved among PurSs and these are located at the interaction site with PurL and PurQ, the other subunits of the formylglycinamide ribonucleotide amidotransferase. Molecular-dynamics simulations of the PurS dimer as well as a model of the complex of the PurS dimer, PurL and PurQ suggest that PurS plays some role in the catalysis of the enzyme by its bending motion. |
| Databáze: | OpenAIRE |
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