Structural classification of biotin carboxyl carrier proteins
Abstract
We gathered primary and tertiary structures of acyl-CoA carboxylases from public databases, and established that members of their biotin carboxylase (BC) and biotin carboxyl carrier protein (BCCP) domains occur in one family each and that members of their carboxyl transferase (CT) domains occur in two families. Protein families have members similar in primary and tertiary structure that probably have descended from the same protein ancestor. The BCCP domains complexed with biotin in acyl and acyl-CoA carboxylases transfer bicarbonate ions from BC domains to CT domains, enabling the latter to carboxylate acyl and acyl-CoA moieties. We separated the BCCP domains into four subfamilies based on more subtle primary structure differences. Members of different BCCP subfamilies often are produced by different types of organisms and are associated with different carboxylases.
Keywords
Acyl-CoA carboxylase Biotin carboxylase carrier protein Primary structure Protein families Tertiary structure ThYmeNotes
Acknowledgments
This work was supported through National Science Foundation Grant EEC-0813570 to the Engineering Research Center for Biorenewable Chemicals, headquartered at Iowa State University and including Pennsylvania State University, Rice University, the University of California, Irvine, the University of New Mexico, the University of Virginia, and the University of Wisconsin-Madison. A. E.-N., an exchange student from the Tecnológico de Monterrey (México), participated in a National Science Foundation Research Experiences for Undergraduates program while being supported by Iowa State University. This article was written while the corresponding author was on a study leave at the School of Chemical Engineering, University of Queensland, Australia. He thanks his colleagues there for their hospitality. The authors thank Bryon Upton (Iowa State University) for his helpful comments.
Supplementary material
References
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