8HUC
Crystal structure of PaIch (Pec1)
Summary for 8HUC
| Entry DOI | 10.2210/pdb8huc/pdb |
| Descriptor | MaoC_dehydrat_N domain-containing protein, GLYCEROL, NITRATE ION, ... (4 entities in total) |
| Functional Keywords | hydro-lyase., unknown function |
| Biological source | Pseudomonas aeruginosa UCBPP-PA14 |
| Total number of polymer chains | 4 |
| Total formula weight | 123826.46 |
| Authors | Pramanik, A.,Datta, S. (deposition date: 2022-12-23, release date: 2023-12-27, Last modification date: 2024-06-26) |
| Primary citation | Pramanik, A.,Datta, S. Structural and functional insights of itaconyl-CoA hydratase from Pseudomonas aeruginosa highlight a novel N-terminal hotdog fold. Febs Lett., 598:1387-1401, 2024 Cited by PubMed Abstract: Itaconyl-CoA hydratase in Pseudomonas aeruginosa (PaIch) converts itaconyl-CoA to (S)-citramalyl-CoA upon addition of a water molecule, a part of an itaconate catabolic pathway in virulent organisms required for their survival in humans host cells. Crystal structure analysis of PaIch showed that a unique N-terminal hotdog fold containing a 4-residue short helical segment α3-, named as an "eaten sausage", followed by a flexible loop region slipped away from the conserved β-sheet scaffold, whereas the C-terminal hotdog fold is similar to all MaoC. A conserved hydratase motif with catalytic residues provides mechanistic insights into catalysis, and existence of a longer substrate binding tunnel may suggest the binding of longer CoA derivatives. PubMed: 38575551DOI: 10.1002/1873-3468.14867 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.984 Å) |
Structure validation
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