5ZW2
FAD complex of PigA
Summary for 5ZW2
| Entry DOI | 10.2210/pdb5zw2/pdb |
| Related | 5ZW0 |
| Descriptor | L-prolyl-[peptidyl-carrier protein] dehydrogenase, FLAVIN-ADENINE DINUCLEOTIDE, 1,4,7,10,13,16-HEXAOXACYCLOOCTADECANE, ... (7 entities in total) |
| Functional Keywords | red pigment, pyrrole, acyl-coa oxidase, fad, tetramer, biosynthetic protein |
| Biological source | Serratia sp. (strain ATCC 39006) |
| Total number of polymer chains | 1 |
| Total formula weight | 45852.31 |
| Authors | Lee, C.-C.,Ko, T.-P.,Wang, A.H.J. (deposition date: 2018-05-14, release date: 2018-09-05, Last modification date: 2023-11-22) |
| Primary citation | Lee, C.-C.,Ko, T.-P.,Chen, C.T.,Chan, Y.T.,Lo, S.Y.,Chang, J.Y.,Chen, Y.W.,Chung, T.F.,Hsieh, H.J.,Hsiao, C.D.,Wang, A.H.J. Crystal Structure of PigA: A Prolyl Thioester-Oxidizing Enzyme in Prodigiosin Biosynthesis. Chembiochem, 20:193-202, 2019 Cited by PubMed Abstract: Prodigiosin is an intensely red pigment comprising three pyrroles. The biosynthetic pathway includes a two-step proline oxidation catalyzed by phosphatidylinositol N-acetylglucosaminyltransferase subunit A (PigA), with flavin adenine dinucleotide (FAD) as its cofactor. The enzyme is crystallized in the apo form and in complex with FAD and proline. As an acyl coenzyme A dehydrogenase (ACAD) family member, the protein folds into a β-sheet flanked by two α-helical domains. PigA forms a tetramer, which is consistent with analytical ultracentrifugation results. FAD binds to PigA in a similar way to that in the other enzymes of the ACAD family. The variable conformations of loop β4-β5 and helix αG correlate well with the structural flexibility required for substrate entrance to the Re side of FAD. Modeling with PigG, the acyl carrier protein, suggests a reasonable mode of interaction with PigA. The structure helps to explain the proline oxidation mechanism, in which Glu244 plays a central role by abstracting the substrate protons. It also reveals a plausible pocket for oxygen binding to the Si side of FAD. PubMed: 30095206DOI: 10.1002/cbic.201800409 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.803 Å) |
Structure validation
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