Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Wu, Hsin-Mao | en_US |
dc.contributor.author | Liu, Sheng-Wen | en_US |
dc.contributor.author | Hsu, Ming-Tsung | en_US |
dc.contributor.author | Hung, Chiu-Lien | en_US |
dc.contributor.author | Lai, Chun-Chieh | en_US |
dc.contributor.author | Cheng, Wen-Chi | en_US |
dc.contributor.author | Wang, Hung-Jung | en_US |
dc.contributor.author | Li, Yaw-Kuen | en_US |
dc.contributor.author | Wang, Wen-Ching | en_US |
dc.date.accessioned | 2014-12-08T15:08:42Z | - |
dc.date.available | 2014-12-08T15:08:42Z | - |
dc.date.issued | 2009-09-25 | en_US |
dc.identifier.issn | 0021-9258 | en_US |
dc.identifier.uri | http://dx.doi.org/10.1074/jbc.M109.010983 | en_US |
dc.identifier.uri | http://hdl.handle.net/11536/6660 | - |
dc.description.abstract | Laminaripentaose-producing beta-1,3-glucanase (LPHase), a member of glycoside hydrolase family 64, cleaves a long-chain polysaccharide beta-1,3-glucan into specific pentasaccharide oligomers. The crystal structure of LPHase from Streptomyces matensis DIC-108 was solved to 1.62 angstrom resolution using multiple-wavelength anomalous dispersion methods. The LPHase structure reveals a novel crescent-like fold; it consists of a barrel domain and a mixed (alpha/beta) domain, forming a wide-open groove between the two domains. The liganded crystal structure was also solved to 1.80 angstrom, showing limited conformational changes. Within the wide groove, a laminaritetraose molecule is found to sit in an electronegatively charged central region and is proximal to several conserved residues including two carboxylates (Glu(154) and Asp(170)) and four other sugar-binding residues (Thr156, Asn(158), Trp(163), and Thr(167)). Molecular modeling using a laminarihexaose as a substrate suggests roles for Glu(154) and Asp(170) as acid and base catalysts, respectively, whereas the side chains of Thr(156), Asn(158), and Trp(163) demarcate subsite +5. Site-directed mutagenesis of Glu(154) and Asp(170) confirms that both carboxylates are essential for catalysis. Together, our results suggest that LPHase uses a direct displacement mechanism involving Glu(154) and Asp(170) to cleave a beta-1,3-glucan into specific alpha-pentasaccharide oligomers. | en_US |
dc.language.iso | en_US | en_US |
dc.title | Structure, Mechanistic Action, and Essential Residues of a GH-64 Enzyme, Laminaripentaose-producing beta-1,3-Glucanase | en_US |
dc.type | Article | en_US |
dc.identifier.doi | 10.1074/jbc.M109.010983 | en_US |
dc.identifier.journal | JOURNAL OF BIOLOGICAL CHEMISTRY | en_US |
dc.citation.volume | 284 | en_US |
dc.citation.issue | 39 | en_US |
dc.citation.spage | 26708 | en_US |
dc.citation.epage | 26715 | en_US |
dc.contributor.department | 應用化學系 | zh_TW |
dc.contributor.department | Department of Applied Chemistry | en_US |
dc.identifier.wosnumber | WOS:000269969600051 | - |
dc.citation.woscount | 6 | - |
Appears in Collections: | Articles |
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