4OOZ

Crystal structure of beta-1,4-D-mannanase from Cryptopygus antarcticus in complex with mannopentaose

Summary for 4OOZ

• Entry DOI: 10.2210/pdb4ooz/pdb
• Related: 4OOU
• Descriptor: Beta-1,4-mannanase, beta-D-mannopyranose-(1-4)-beta-D-mannopyranose-(1-4)-beta-D-mannopyranose-(1-4)-beta-D-mannopyranose, beta-D-mannopyranose-(1-4)-beta-D-mannopyranose-(1-4)-beta-D-mannopyranose-(1-4)-beta-D-mannopyranose-(1-4)-beta-D-mannopyranose, ... (5 entities in total)
• Functional Keywords: tim barrel, hydrolase
• Biological source: Cryptopygus antarcticus
• Total number of polymer chains: 2
• Total formula weight: 88741.37

Authors

Kim, M.-K.,An, Y.J.,Jeong, C.-S.,Cha, S.-S. (deposition date: 2014-02-04, release date: 2014-08-06, Last modification date: 2024-10-16)

Primary citation

Kim, M.K.,An, Y.J.,Song, J.M.,Jeong, C.S.,Kang, M.H.,Kwon, K.K.,Lee, Y.H.,Cha, S.S.
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, 82:3217-3223, 2014

PubMed 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.

PubMed: 25082572
DOI: 10.1002/prot.24655

Experimental method

X-RAY DIFFRACTION (2.6 Å)