Structural and functional insights of itaconyl‐CoA hydratase from Pseudomonas aeruginosa highlight a novel N‐terminal hotdog fold

Author:

Pramanik Atanu1,Datta Saumen12ORCID

Affiliation:

1. Department of Structural Biology and Bio‐informatics CSIR‐Indian Institute of Chemical Biology (CSIR‐IICB) Kolkata India

2. Biological Sciences Academy of Scientific and Innovative Research (AcSIR) Ghaziabad India

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.

Publisher

Wiley

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