6p5u

Revision as of 10:23, 11 October 2023 by OCA (talk | contribs)
(diff) ← Older revision | Latest revision (diff) | Newer revision → (diff)

Structure of an enoyl-CoA hydratase/aldolase isolated from a lignin-degrading consortiumStructure of an enoyl-CoA hydratase/aldolase isolated from a lignin-degrading consortium

Structural highlights

6p5u is a 6 chain structure with sequence from Uncultured organism. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.1Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

A0A2P1BT02_9ZZZZ

Publication Abstract from PubMed

In the context of increasing demand for renewable alternatives of fuels and chemicals, the valorization of lignin emerges as a value-adding strategy in biorefineries and an alternative to petroleum-derived molecules. One of the compounds derived from lignin is ferulic acid (FA), which can be converted into valuable molecules such as vanillin. In microorganisms, FA biotransformation into vanillin can occur via a two-step reaction catalyzed by the sequential activity of a feruloyl-CoA synthetase (FCS) and an feruloyl-CoA hydratase-lyase (FCHL), which could be exploited industrially. In this study, a prokaryotic FCHL derived from a lignin-degrading microbial consortium (named LM-FCHL) was cloned, successfully expressed in soluble form and purified. The crystal structure was solved and refined at 2.1 A resolution. The LM-FCHL is a hexamer composed of a dimer of trimers, which showed to be quite stable under extreme pH conditions. Finally, small angle X-ray scattering corroborates the hexameric state in solution and indicates flexibility in the protein structure. The present study contributes to the field of lignin valorization to valuable molecules by establishing the biophysical and structural characterization for a novel FCHL member of unique characteristics.

The structure of a prokaryotic feruloyl-CoA hydratase-lyase from a lignin-degrading consortium with high oligomerization stability under extreme pHs.,Liberato MV, Araujo JN, Sodre V, Goncalves TA, Vilela N, Moraes EC, Garcia W, Squina FM Biochim Biophys Acta Proteins Proteom. 2020 Mar;1868(3):140344. doi:, 10.1016/j.bbapap.2019.140344. Epub 2019 Dec 10. PMID:31841665[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Liberato MV, Araujo JN, Sodre V, Goncalves TA, Vilela N, Moraes EC, Garcia W, Squina FM. The structure of a prokaryotic feruloyl-CoA hydratase-lyase from a lignin-degrading consortium with high oligomerization stability under extreme pHs. Biochim Biophys Acta Proteins Proteom. 2020 Mar;1868(3):140344. doi:, 10.1016/j.bbapap.2019.140344. Epub 2019 Dec 10. PMID:31841665 doi:http://dx.doi.org/10.1016/j.bbapap.2019.140344

6p5u, resolution 2.10Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA