Structural highlights
Publication Abstract from PubMed
Endo-beta-1,4-d-mannanase from the Antarctic springtail, Cryptopygus antarcticus (CaMan), is a cold-adapted beta-mannanase that has the lowest optimum temperature (30 degrees C) of all known beta-mannanases. Here, we report the apo- and mannopentaose (M5) complex structures of CaMan. Structural comparison of CaMan with other beta-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.
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.,Kim MK, An YJ, Song JM, Jeong CS, Kang MH, Kwon KK, Lee YH, Cha SS Proteins. 2014 Nov;82(11):3217-23. doi: 10.1002/prot.24655. Epub 2014 Aug 19. PMID:25082572[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kim MK, An YJ, Song JM, Jeong CS, Kang MH, Kwon KK, Lee YH, Cha SS. 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. Proteins. 2014 Nov;82(11):3217-23. doi: 10.1002/prot.24655. Epub 2014 Aug 19. PMID:25082572 doi:http://dx.doi.org/10.1002/prot.24655
