6KSY
Crystal structure of arginase from Zymomonas mobilis ZM4
Summary for 6KSY
| Entry DOI | 10.2210/pdb6ksy/pdb |
| Descriptor | Arginase/agmatinase/formiminoglutamase, ZINC ION (3 entities in total) |
| Functional Keywords | arginase, hydrolase |
| Biological source | Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) |
| Total number of polymer chains | 4 |
| Total formula weight | 129142.23 |
| Authors | Park, S.Y.,Hwangbo, S.A. (deposition date: 2019-08-26, release date: 2020-08-05, Last modification date: 2024-03-27) |
| Primary citation | Hwangbo, S.A.,Kim, J.W.,Jung, S.J.,Jin, K.S.,Lee, J.O.,Kim, J.S.,Park, S.Y. Characterization of a Dimeric Arginase FromZymomonas mobilisZM4. Front Microbiol, 10:2755-2755, 2019 Cited by PubMed Abstract: Many organisms have genes to protect themselves from toxic conditions such as high ethanol and/or ammonia concentrations. When a high ethanol condition is induced to ZM4, a representative ethanologenic organism, this bacterium overexpresses several genes to overcome this ethanol stress. Among them, we characterized a gene product annotated as an arginase (zmARG) from ZM4. Even though all of the arginase-determining sequence motifs are not strictly conserved in zmARG, this enzyme converts L-arginine to urea and L-ornithine in the presence of a divalent manganese ion. The revealed high-resolution crystal structure of zmARG shows that it has a typical globular α/β arginase fold with a protruded C-terminal helix. Two zinc ions reside in the active site, where one metal ion is penta-coordinated and the other has six ligands, discerning this zmARG from the reported arginases with two hexa-liganded metal ions. zmARG forms a dimeric structure in solution as well as in the crystalline state. The dimeric assembly of zmARG is formed mainly by interaction formed between the C-terminal α-helix of one molecule and the α/β hydrolase fold of another molecule. The presented findings demonstrate the first reported dimeric arginase formed by the C-terminal tail and has two metal ions coordinated by different number of ligands. PubMed: 32038508DOI: 10.3389/fmicb.2019.02755 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.649 Å) |
Structure validation
Download full validation report
