1MJH
Structure-based assignment of the biochemical function of hypothetical protein MJ0577: A test case of structural genomics
Summary for 1MJH
Entry DOI | 10.2210/pdb1mjh/pdb |
Descriptor | PROTEIN (ATP-BINDING DOMAIN OF PROTEIN MJ0577), MANGANESE (II) ION, ADENOSINE-5'-TRIPHOSPHATE, ... (4 entities in total) |
Functional Keywords | hypothetical protein, structural genomics, functional assignment, atp binding protein, bsgc structure funded by nih, protein structure initiative, psi, berkeley structural genomics center |
Biological source | Methanocaldococcus jannaschii |
Cellular location | Cytoplasm: Q57997 |
Total number of polymer chains | 2 |
Total formula weight | 37865.44 |
Authors | Zarembinski, T.I.,Hung, L.-W.,Mueller-Dieckmann, H.J.,Kim, K.-K.,Yokota, H.,Kim, R.,Kim, S.-H.,Berkeley Structural Genomics Center (BSGC) (deposition date: 1998-11-04, release date: 1998-12-23, Last modification date: 2023-12-27) |
Primary citation | Zarembinski, T.I.,Hung, L.-W.,Mueller-Dieckmann, H.J.,Kim, K.-K.,Yokota, H.,Kim, R.,Kim, S.-H. Structure-based assignment of the biochemical function of a hypothetical protein: a test case of structural genomics. Proc.Natl.Acad.Sci.USA, 95:15189-15193, 1998 Cited by PubMed Abstract: Many small bacterial, archaebacterial, and eukaryotic genomes have been sequenced, and the larger eukaryotic genomes are predicted to be completely sequenced within the next decade. In all genomes sequenced to date, a large portion of these organisms' predicted protein coding regions encode polypeptides of unknown biochemical, biophysical, and/or cellular functions. Three-dimensional structures of these proteins may suggest biochemical or biophysical functions. Here we report the crystal structure of one such protein, MJ0577, from a hyperthermophile, Methanococcus jannaschii, at 1.7-A resolution. The structure contains a bound ATP, suggesting MJ0577 is an ATPase or an ATP-mediated molecular switch, which we confirm by biochemical experiments. Furthermore, the structure reveals different ATP binding motifs that are shared among many homologous hypothetical proteins in this family. This result indicates that structure-based assignment of molecular function is a viable approach for the large-scale biochemical assignment of proteins and for discovering new motifs, a basic premise of structural genomics. PubMed: 9860944DOI: 10.1073/pnas.95.26.15189 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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