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 |
| |
| Authors: | Min‐Kyu Kim Young Jun An Jung Min Song Chang‐Sook Jeong Mee Hye Kang Kae Kyoung Kwon Youn‐Ho Lee Sun‐Shin Cha |
| |
| Institution: | 1. Marine Biotechnology Research Division, Korea Institute of Ocean Science and Technology, , Ansan, 426–744 Republic of Korea;2. Marine Ecosystem Research Division, Korea Institute of Ocean Science and Technology, , Ansan, 426–744 Republic of Korea;3. Department of Convergence Study on the Ocean Science and Technology, Ocean Science and Technology School, Korea Maritime and Ocean University, , Pusan, 606–791 Republic of Korea;4. Department of Marine Biotechnology, University of Science and Technology, , DaeJeon, 305–333 Republic of Korea |
| |
| 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. Proteins 2014; 82:3217–3223. © 2014 Wiley Periodicals, Inc. |
| |
| Keywords: | β ‐mannanase CaMan GH5 mannan cold‐adaptation Cryptopygus antarcticus |
|
|
