Summary for 7E3V
| Entry DOI | 10.2210/pdb7e3v/pdb |
| Descriptor | UPF0173 metal-dependent hydrolase C7P97_11315, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, CHLORIDE ION, ... (6 entities in total) |
| Functional Keywords | dnase, rnase, phosphodiesterase, metal binding protein |
| Biological source | Staphylococcus aureus |
| Total number of polymer chains | 6 |
| Total formula weight | 165104.84 |
| Authors | Lee, K.-Y.,Kim, D.-G.,Lee, B.-J. (deposition date: 2021-02-09, release date: 2022-02-23, Last modification date: 2023-11-29) |
| Primary citation | Kim, D.G.,Lee, K.Y.,Lee, S.J.,Cheon, S.H.,Choi, Y.,Lee, H.H.,Ahn, H.C.,Lee, B.J. Structural and functional studies of SAV1707 from Staphylococcus aureus elucidate its distinct metal-dependent activity and a crucial residue for catalysis. Acta Crystallogr D Struct Biol, 77:587-598, 2021 Cited by PubMed Abstract: The metallo-β-lactamase fold is the most abundant metal-binding domain found in two major kingdoms: bacteria and archaea. Despite the rapid growth in genomic information, most of these enzymes, which may play critical roles in cellular metabolism, remain uncharacterized in terms of structure and function. In this study, X-ray crystal structures of SAV1707, a hypothetical metalloenzyme from Staphylococcus aureus, and its complex with cAMP are reported at high resolutions of 2.05 and 1.55 Å, respectively, with a detailed atomic description. Through a functional study, it was verified that SAV1707 has Ni-dependent phosphodiesterase activity and Mn-dependent endonuclease activity, revealing a different metal selectivity depending on the reaction. In addition, the crystal structure of cAMP-bound SAV1707 shows a unique snapshot of cAMP that reveals the binding mode of the intermediate, and a key residue Phe511 that forms π-π interactions with cAMP was verified as contributing to substrate recognition by functional studies of its mutant. Overall, these findings characterized the relationship between the structure and function of SAV1707 and may provide further understanding of metalloenzymes possessing the metallo-β-lactamase fold. PubMed: 33950015DOI: 10.1107/S2059798321001923 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.05 Å) |
Structure validation
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