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. Issue 11 (19th August 2014)

• Record Type: Journal Article
• Authors: Kim, Min‐Kyu; An, Young Jun; Song, Jung Min; Jeong, Chang‐Sook; Kang, Mee Hye; Kwon, Kae Kyoung; Lee, Youn‐Ho; Cha, Sun‐Shin
• Is Part Of: Proteins. Volume 82:Issue 11(2014)
• Page Start: 3217
• Page End: 3223
• Publication Date: 2014-08-19
• Subjects: Proteins -- Periodicals; Proteins -- Periodicals; 572.6
• DOI: 10.1002/prot.24655
• Languages: English
• ISSNs: 0887-3585

Abstract

<abstract abstract-type="main"> <title>ABSTRACT</title> <p>Endo‐β‐1, 4‐<sc>d</sc>‐mannanase from the Antarctic springtail, <italic>Cryptopygus antarcticus</italic> (<italic>Ca</italic>Man), 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 <italic>Ca</italic>Man. Structural comparison of <italic>Ca</italic>Man with other β‐mannanases from the multicellular animals reveals that <italic>Ca</italic>Man 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 <italic>Ca</italic>Man‐M5 complex structure, we defined the mannose‐recognition subsites and observed unreported M5 binding site on the surface of <italic>Ca</italic>Man. Proteins 2014; 82:3217–3223. © 2014 Wiley Periodicals, Inc.</p> </abstract>