6AF6

PigA with FAD and proline

6AF6 の概要

• エントリーDOI: 10.2210/pdb6af6/pdb
• 関連するPDBエントリー: 5zw0 5zw2 5zw7 5zw8
• 分子名称: L-prolyl-[peptidyl-carrier protein] dehydrogenase, FLAVIN-ADENINE DINUCLEOTIDE, 1,4,7,10,13,16-HEXAOXACYCLOOCTADECANE, ... (7 entities in total)
• 機能のキーワード: red pigment, pyrrole, acyl-coa oxidase, fad, tetramer, biosynthetic protein
• 由来する生物種: Serratia sp. (strain ATCC 39006)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 45547.04

構造登録者

Lee, C.-C.,Ko, T.-P.,Wang, A.H.J. (登録日: 2018-08-08, 公開日: 2018-09-05, 最終更新日: 2023-11-22)

主引用文献

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

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: 30095206
DOI: 10.1002/cbic.201800409

実験手法

X-RAY DIFFRACTION (1.62 Å)