Methods for Structural and Functional Analyses of Intramembrane Prenyltransferases in the UbiA Superfamily

Y. Yang, N. Ke, S. Liu, W. Li

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

4 Scopus citations

Abstract

The UbiA superfamily is a group of intramembrane prenyltransferases that generate lipophilic compounds essential in biological membranes. These compounds, which include various quinones, hemes, chlorophylls, and vitamin E, participate in electron transport and function as antioxidants, as well as acting as structural lipids of microbial cell walls and membranes. Prenyltransferases producing these compounds are involved in important physiological processes and human diseases. These UbiA superfamily members differ significantly in their enzymatic activities and substrate selectivities. This chapter describes examples of methods that can be used to group these intramembrane enzymes, analyze their activity, and screen and crystallize homolog proteins for structure determination. Recent structures of two archaeal homologs are compared with structures of soluble prenyltransferases to show distinct mechanisms used by the UbiA superfamily to control enzymatic activity in membranes.

Original languageEnglish
Title of host publicationMethods in Enzymology
PublisherAcademic Press Inc.
Pages309-347
Number of pages39
DOIs
StatePublished - 2017

Publication series

NameMethods in Enzymology
Volume584
ISSN (Print)0076-6879
ISSN (Electronic)1557-7988

Keywords

  • COQ2
  • Crystal structures
  • Crystallography
  • Intramembrane enzymes
  • Liquid cubic phase
  • Membrane proteins
  • Prenyltransferases
  • Quinones
  • Sequence clustering
  • Structural lipids
  • UBIAD1
  • UbiA

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