Architecture of multienzyme complex in action: polyketide synthase

Article in Nature, Vol. 531, 24 March 2016, pp. 533, “Mycocerosic acid synthase exemplifies the architecture of reducing polyketide synthases”

 

Summary of article: Various domains of polyketide synthases were crystallized individually or as segments, and the overall structure of the enzyme complex elucidated. While the method used structures of individual subunits to reconstruct the overall structure of a multi-subunit enzyme complex that has thus far proved difficult to solve, the residual error likely inherent in the reconstruction effort may hamper understanding of the enzyme’s function in action. Specifically, failure to crystallize the entire enzyme complex (whether bound or not bound to a substrate) meant that it is not possible to understand, in totality, the function of various subunits and domains of the enzyme in biocatalysis. Hence, while the paper is an advance in our understanding of the role and functions of various subunits and their domains in catalysis by mycocerosic acid synthase, the lack of a holistic structural picture of the enzyme complex meant that the elucidated understanding of the various subunits’ roles in catalysis remain as postulations waiting to be verified by other studies that may yield information on the structure of the entire enzyme system.

 

Link to original article: http://www.nature.com/nature/journal/v531/n7595/full/nature16993.html?foxtrotcallback=true

 

Category: Interesting scientific articles, biochemistry, molecular biology, biophysics, structural biology, bioengineering,

Tags: polyketide synthase, protein crystallization, function, structure, multi-subunit enzyme,

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