Mitochondrial Pyruvate Carrier 1 and 2 Heterodimer, In Silico, Models of Plant and Human Complexes: A Comparison of Structure and Transporter Binding Properties

Mitochondrial Pyruvate Carrier 1 and 2 Heterodimer, In Silico, Models of Plant and Human Complexes: A Comparison of Structure and Transporter Binding Properties

Jason L. Dugan (University of Texas at San Antonio, San Antonio, Texas, United States), Allen K. Bourdon (University of Tennessee at Knoxville, Knoxville, Tennessee, United States) and Clyde F. Phelix (University of Texas at San Antonio, San Antonio, Texas, United States)
Copyright: © 2017 |Pages: 32
DOI: 10.4018/IJKDB.2017070102
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Abstract

The plant and human mitochondrial pyruvate carrier (MPC) had been studied in the 1970s-1990s providing many predictions on functional protein structure and mechanisms of substrate binding. Genes for human and plant MPC have been identified, but no crystal structure has yet been registered or deposited in a protein data bank. This report describes results for comparisons of structure for human and plant MPC1/2 heterodimer homology models. Key cysteine residues are identified for pyruvate and blocker binding and formation of thiohemiacetal or Michael addition bonds. Evidence is provided for an alternating access model in human, mouse ear-cress, castor and common beans, and corn.
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Introduction

Plant mitochondrial pyruvate carrier (MPC) had been studied for many years, decades ago (Beechey, Brailsford, & Thompson, 1987; Brailsford, Thompson, Kaderbhai, & Beechey, 1986a, 1986b; Day & Hanson, 1977; Laloi, 1999; Proudlove, Beechey, & Moore, 1987b; Walker & Beevers, 1956), but the plant genes have only recently been discovered (C. Li, Wang, Ma, & Zhang, 2014; M. Wang, Ma, Shen, Li, & Zhang, 2014). There is a role of MPC complex in the abscisic acid (ABA) mediated stomata opening and closing during environmental stress (Santelia & Lawson, 2016; Yu & Assmann, 2014), in addition to energy production, primary metabolism and carbon flux in general. Inner mitochondrial membrane proteins are transported across mitochondrial membranes in plants (Alberts, Johnson, & Lewis, 2002; Duncan, Murcha, & Whelan, 2013; Murcha et al., 2014) similar to that in humans (Kühlbrandt, 2015; Neupert & Herrmann, 2007); indicating that the structural characteristics of the functional proteins might be similar. Overall, this information is useful for in silico biosimulations of metabolism in plants (Beckers et al., 2016; Phelix & Feltus, 2014) and humans (Hammack, Perry, LeBaron, Villareal, & Phelix, 2015; Phelix, Bourdon, Villareal, & LeBaron, 2016; Phelix & Dugan, 2016; Phelix, Villareal, LeBaron, Perry, & Roberson, 2014). For Arabidopsis thaliana and Zea mays this is particularly interesting because full genome-scale metabolic networks are available (Beckers et al., 2016; Saha, Suthers, & Maranas, 2011; Seaver et al., 2015). Understanding membrane transport of pyruvate in plants is critical to engineering plant primary metabolism, in particular for oils and biodiesel production (Lin et al., 2017; Schwender et al., 2015; Weber & Bräutigam, 2013).

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