Structure-based investigation into the functional roles of the extended loop and substrate-recognition sites in an endo-β-1,4-D-mannanase from the Antarctic springtail, Cryptopygus antarcticus

Min Kyu Kim, Young Jun An, Jung Min Song, Chang Sook Jeong, Mee Hye Kang, Kae Kyoung Kwon, Youn Ho Lee, Sun Shin Cha

Research output: Contribution to journalArticle

10 Scopus citations

Abstract

Endo-β-1,4-d-mannanase from the Antarctic springtail, Cryptopygus antarcticus (CaMan), is a cold-adapted β-mannanase that has the lowest optimum temperature (30°C) of all known β-mannanases. Here, we report the apo- and mannopentaose (M5) complex structures of CaMan. Structural comparison of CaMan with other β-mannanases from the multicellular animals reveals that CaMan has an extended loop that alters topography of the active site. Structural and mutational analyses suggest that this extended loop is linked to the cold-adapted enzymatic activity. From the CaMan-M5 complex structure, we defined the mannose-recognition subsites and observed unreported M5 binding site on the surface of CaMan. ss

Original languageEnglish (US)
Pages (from-to)3217-3223
Number of pages7
JournalProteins: Structure, Function and Bioinformatics
Volume82
Issue number11
DOIs
StatePublished - Jan 1 2014

Keywords

  • CaMan
  • Cold-adaptation
  • Cryptopygus antarcticus
  • GH5
  • Mannan
  • β-mannanase

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