scholarly journals Crystal structure and functional characterization of a cold-active acetyl xylan esterase (PbAcE) from psychrophilic soil microbe Paenibacillus sp.

PLoS ONE ◽  
2018 ◽  
Vol 13 (10) ◽  
pp. e0206260 ◽  
Author(s):  
Sun-Ha Park ◽  
Wanki Yoo ◽  
Chang Woo Lee ◽  
Chang Sook Jeong ◽  
Seung Chul Shin ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Functional Characterization ◽  
Acetyl Xylan Esterase ◽  
Soil Microbe ◽  
Paenibacillus Sp ◽  
Cold Active

Structural and functional characterization of a glycoside hydrolase family 3 β-N-acetylglucosaminidase from Paenibacillus sp. str. FPU-7

2019 ◽  
Vol 166 (6) ◽  
pp. 503-515
Author(s):  
Takafumi Itoh ◽  
Tomomitsu Araki ◽  
Tomohiro Nishiyama ◽  
Takao Hibi ◽  
Hisashi Kimoto
Keyword(s):  
Crystal Structure ◽  
Glycoside Hydrolase ◽  
Catalytic Mechanism ◽  
Functional Characterization ◽  
Structural Features ◽  
Expression Cloning ◽  
Glycoside Hydrolase Family ◽  
Paenibacillus Sp ◽  
Hydrolase Family

Abstract Chitin, a β-1,4-linked homopolysaccharide of N-acetyl-d-glucosamine (GlcNAc), is one of the most abundant biopolymers on Earth. Paenibacillus sp. str. FPU-7 produces several different chitinases and converts chitin into N,N′-diacetylchitobiose ((GlcNAc)2) in the culture medium. However, the mechanism by which the Paenibacillus species imports (GlcNAc)2 into the cytoplasm and divides it into the monomer GlcNAc remains unclear. The gene encoding Paenibacillus β-N-acetyl-d-glucosaminidase (PsNagA) was identified in the Paenibacillus sp. str. FPU-7 genome using an expression cloning system. The deduced amino acid sequence of PsNagA suggests that the enzyme is a part of the glycoside hydrolase family 3 (GH3). Recombinant PsNagA was successfully overexpressed in Escherichia coli and purified to homogeneity. As assessed by gel permeation chromatography, the enzyme exists as a 57-kDa monomer. PsNagA specifically hydrolyses chitin oligosaccharides, (GlcNAc)2–4, 4-nitrophenyl N-acetyl β-d-glucosamine (pNP-GlcNAc) and pNP-(GlcNAc)2–6, but has no detectable activity against 4-nitrophenyl β-d-glucose, 4-nitrophenyl β-d-galactosamine and colloidal chitin. In this study, we present a 1.9 Å crystal structure of PsNagA bound to GlcNAc. The crystal structure reveals structural features related to substrate recognition and the catalytic mechanism of PsNagA. This is the first study on the structural and functional characterization of a GH3 β-N-acetyl-d-glucosaminidase from Paenibacillus sp.

scholarly journals Crystal Structure and Functional Characterization of the Complement Regulator Mannose-binding Lectin (MBL)/Ficolin-associated Protein-1 (MAP-1)

2012 ◽  
Vol 287 (39) ◽  
pp. 32913-32921 ◽  
Author(s):  
Mikkel-Ole Skjoedt ◽  
Pietro Roversi ◽  
Tina Hummelshøj ◽  
Yaseelan Palarasah ◽  
Anne Rosbjerg ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Functional Characterization ◽  
Mannose Binding Lectin ◽  
Mannose Binding ◽  
Complement Regulator ◽  
Binding Lectin

scholarly journals Crystal structure and functional characterization of a light-driven chloride pump having an NTQ motif

2016 ◽  
Vol 7 (1) ◽  
Author(s):  
Kuglae Kim ◽  
Soon-Kyeong Kwon ◽  
Sung-Hoon Jun ◽  
Jeong Seok Cha ◽  
Hoyoung Kim ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Functional Characterization ◽  
Chloride Pump

scholarly journals Crystal Structure and Functional Characterization of an Esterase (EaEST) from Exiguobacterium antarcticum

PLoS ONE ◽  
2017 ◽  
Vol 12 (1) ◽  
pp. e0169540 ◽  
Author(s):  
Chang Woo Lee ◽  
Sena Kwon ◽  
Sun-Ha Park ◽  
Boo-Young Kim ◽  
Wanki Yoo ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Functional Characterization ◽  
Exiguobacterium Antarcticum

Cloning and functional characterization of a complex endo-β-1,3-glucanase from Paenibacillus sp.

2009 ◽  
Vol 81 (6) ◽  
pp. 1051-1061 ◽  
Author(s):  
Yueh-Mei Cheng ◽  
Tang-Yao Hong ◽  
Chia-Chi Liu ◽  
Menghsiao Meng
Keyword(s):  
Functional Characterization ◽  
Paenibacillus Sp

scholarly journals Functional characterization of heat-shock protein 90 fromOryza sativaand crystal structure of its N-terminal domain

2015 ◽  
Vol 71 (6) ◽  
pp. 688-696 ◽  
Author(s):  
Swetha Raman ◽  
Kaza Suguna
Keyword(s):  
Crystal Structure ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Biochemical Characterization ◽  
Functional Characterization ◽  
Cell Signalling ◽  
Physiological Role ◽  
Heat Shock Protein 90 ◽  
Terminal Domain

Heat-shock protein 90 (Hsp90) is an ATP-dependent molecular chaperone that is essential for the normal functioning of eukaryotic cells. It plays crucial roles in cell signalling, cell-cycle control and in maintaining proteome integrity and protein homeostasis. In plants, Hsp90s are required for normal plant growth and development. Hsp90s are observed to be upregulated in response to various abiotic and biotic stresses and are also involved in immune responses in plants. Although there are several studies elucidating the physiological role of Hsp90s in plants, their molecular mechanism of action is still unclear. In this study, biochemical characterization of an Hsp90 protein from rice (Oryza sativa; OsHsp90) has been performed and the crystal structure of its N-terminal domain (OsHsp90-NTD) was determined. The binding of OsHsp90 to its substrate ATP and the inhibitor 17-AAG was studied by fluorescence spectroscopy. The protein also exhibited a weak ATPase activity. The crystal structure of OsHsp90-NTD was solved in complex with the nonhydrolyzable ATP analogue AMPPCP at 3.1 Å resolution. The domain was crystallized by cross-seeding with crystals of the N-terminal domain of Hsp90 fromDictyostelium discoideum, which shares 70% sequence identity with OsHsp90-NTD. This is the second reported structure of a domain of Hsp90 from a plant source.

Identification and Functional Characterization of an α-Amylase with Broad Temperature and pH Stability from Paenibacillus sp.

2013 ◽  
Vol 170 (2) ◽  
pp. 359-369 ◽  
Author(s):  
Thangamani Rajesh ◽  
Yong Hyun Kim ◽  
Yong-Keun Choi ◽  
Jong Min Jeon ◽  
Hyun Joong Kim ◽  
...  
Keyword(s):  
Functional Characterization ◽  
Ph Stability ◽  
Paenibacillus Sp

Structural and functional characterization of an Isd-type haem-degradation enzyme fromListeria monocytogenes

2014 ◽  
Vol 70 (3) ◽  
pp. 615-626 ◽  
Author(s):  
Thao Duong ◽  
Kwangsu Park ◽  
Truc Kim ◽  
Sung Wook Kang ◽  
Myung Joon Hahn ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Degradation Product ◽  
Functional Characterization ◽  
Human Pathogen ◽  
Monooxygenase Activity ◽  
Gram Positive Bacteria ◽  
Functional Assays ◽  
Terminal Domain ◽  
Life Threatening

Bacterial pathogens have evolved diverse types of efficient machinery to acquire haem, the most abundant source of iron in the human body, and degrade it for the utilization of iron. Gram-positive bacteria commonly encode IsdG-family proteins as haem-degrading monooxygenases.Listeria monocytogenesis predicted to possess an IsdG-type protein (Lmo2213), but the residues involved in haem monooxygenase activity are not well conserved and there is an extra N-terminal domain in Lmo2213. Therefore, its function and mechanism of action cannot be predicted. In this study, the crystal structure of Lmo2213 was determined at 1.75 Å resolution and its haem-binding and haem-degradation activities were confirmed. Structure-based mutational and functional assays of this protein, designated as an Isd-typeL. monocytogeneshaem-degrading enzyme (Isd-LmHde), identified that Glu71, Tyr87 and Trp129 play important roles in haem degradation and that the N-terminal domain is also critical for its haem-degrading activity. The haem-degradation product of Isd-LmHde is verified to be biliverdin, which is also known to be the degradation product of other bacterial haem oxygenases. This study, the first structural and functional report of the haem-degradation system inL. monocytogenes, sheds light on the concealed haem-utilization system in this life-threatening human pathogen.

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