Structure-based investigation into the functional roles of the extended loop and substrate-recognition sites in an endo-beta-1,4-D-mannanase from the Antarctic springtail, Cryptopygus antarcticus SCIE SCOPUS
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- Title
- Structure-based investigation into the functional roles of the extended loop and substrate-recognition sites in an endo-beta-1,4-D-mannanase from the Antarctic springtail, Cryptopygus antarcticus
- KIOST Author(s)
- An, Young Jun(안영준); Kwon, Kae Kyoung(권개경); Lee, Youn Ho(이윤호)
- Alternative Author(s)
- 김민규; 안영준; 송정민; 정창숙; 강미혜; 권개경; 이윤호; 차선신
- Publication Year
- 2014-11
- Abstract
- Endo-beta-1,4-d-mannanase from the Antarctic springtail, Cryptopygus antarcticus (CaMan), is a cold-adapted -mannanase that has the lowest optimum temperature (30 degrees C) of all known -mannanases. Here, we report the apo- and mannopentaose (M5) complex structures of CaMan. Structural comparison of CaMan with other -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. Proteins 2014; 82:3217-3223. (c) 2014 Wiley Periodicals, Inc.
- ISSN
- 0887-3585
- Bibliographic Citation
- PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, v.82, no.11, pp.3217 - 3223, 2014
- Publisher
- WILEY
- Subject
- COLD-ACTIVE BETA-1,4-D-MANNANASE; CRYSTAL-STRUCTURE; BETA-MANNANASE; ALPHA-AMYLASE; DOMAIN-C; SPECIFICITY; PROTEINS; RESIDUES; COMPLEX; BINDING
- Keywords
- beta-mannanase; CaMan; GH5; mannan; cold-adaptation; Cryptopygus antarcticus
- Type
- Article
- Language
- English
- Document Type
- Article
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- There are no files associated with this item.
