1OKJ
crystal structure of the essential E. coli YeaZ protein by MAD method using the gadolinium complex "DOTMA"
Summary for 1OKJ
| Entry DOI | 10.2210/pdb1okj/pdb |
| Descriptor | TRNA THREONYLCARBAMOYLADENOSINE BIOSYNTHESIS PROTEIN TSAB, GADOLINIUM ION (3 entities in total) |
| Functional Keywords | potential zinc protease, hypothetical protease yeaz, metalloprotease, hydrolase, bacterial targets at igs-cnrs, france, bigs, structural genomics |
| Biological source | ESCHERICHIA COLI |
| Cellular location | Cytoplasm: P76256 |
| Total number of polymer chains | 4 |
| Total formula weight | 111695.52 |
| Authors | Abergel, C.,Jeudy, S.,Claverie, J.M. (deposition date: 2003-07-26, release date: 2004-09-16, Last modification date: 2024-11-20) |
| Primary citation | Stelter, M.,Molina, R.,Jeudy, S.,Kahn, R.,Abergel, C.,Hermoso, J.A. A Complement to the Modern Crystallographer'S Toolbox: Caged Gadolinium Complexes with Versatile Binding Modes. Acta Crystallogr.,Sect.D, 70:1506-, 2014 Cited by PubMed Abstract: A set of seven caged gadolinium complexes were used as vectors for introducing the chelated Gd(3+) ion into protein crystals in order to provide strong anomalous scattering for de novo phasing. The complexes contained multidentate ligand molecules with different functional groups to provide a panel of possible interactions with the protein. An exhaustive crystallographic analysis showed them to be nondisruptive to the diffraction quality of the prepared derivative crystals, and as many as 50% of the derivatives allowed the determination of accurate phases, leading to high-quality experimental electron-density maps. At least two successful derivatives were identified for all tested proteins. Structure refinement showed that the complexes bind to the protein surface or solvent-accessible cavities, involving hydrogen bonds, electrostatic and CH-π interactions, explaining their versatile binding modes. Their high phasing power, complementary binding modes and ease of use make them highly suitable as a heavy-atom screen for high-throughput de novo structure determination, in combination with the SAD method. They can also provide a reliable tool for the development of new methods such as serial femtosecond crystallography. PubMed: 24914962DOI: 10.1107/S1399004714005483 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.28 Å) |
Structure validation
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