4WWZ
UndA complexed with 2,3-dodecenoic acid
Summary for 4WWZ
| Entry DOI | 10.2210/pdb4wwz/pdb |
| Related | 4WWJ 4WX0 |
| Descriptor | TENA/THI-4 family protein, FE (III) ION, (2E)-dodec-2-enoic acid, ... (7 entities in total) |
| Functional Keywords | non-heme iron dependent desaturase/decarboxylase, 1-undecene biosynthesis, aliphatic medium-chain 1-alkene biosynthesis, metalloenzyme, oxidoreductase |
| Biological source | Pseudomonas protegens Pf-5 |
| Total number of polymer chains | 2 |
| Total formula weight | 62364.41 |
| Authors | Li, X.,Cate, J.D.H. (deposition date: 2014-11-13, release date: 2014-12-24, Last modification date: 2024-02-28) |
| Primary citation | Rui, Z.,Li, X.,Zhu, X.,Liu, J.,Domigan, B.,Barr, I.,Cate, J.H.,Zhang, W. Microbial biosynthesis of medium-chain 1-alkenes by a nonheme iron oxidase. Proc.Natl.Acad.Sci.USA, 111:18237-18242, 2014 Cited by PubMed Abstract: Aliphatic medium-chain 1-alkenes (MCAEs, ∼10 carbons) are "drop-in" compatible next-generation fuels and precursors to commodity chemicals. Mass production of MCAEs from renewable resources holds promise for mitigating dependence on fossil hydrocarbons. An MCAE, such as 1-undecene, is naturally produced by Pseudomonas as a semivolatile metabolite through an unknown biosynthetic pathway. We describe here the discovery of a single gene conserved in Pseudomonas responsible for 1-undecene biosynthesis. The encoded enzyme is able to convert medium-chain fatty acids (C10-C14) into their corresponding terminal olefins using an oxygen-activating, nonheme iron-dependent mechanism. Both biochemical and X-ray crystal structural analyses suggest an unusual mechanism of β-hydrogen abstraction during fatty acid substrate activation. Our discovery unveils previously unidentified chemistry in the nonheme Fe(II) enzyme family, provides an opportunity to explore the biology of 1-undecene in Pseudomonas, and paves the way for tailored bioconversion of renewable raw materials to MCAE-based biofuels and chemical commodities. PubMed: 25489112DOI: 10.1073/pnas.1419701112 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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