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Tytuł:
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Crystal structure of a novel putative sugar isomerase from the psychrophilic bacterium Paenibacillus sp. R4.
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Autorzy:
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Kwon S; Department of Biotechnology, Konkuk University, Chungju, Chungbuk, 27478, Republic of Korea.
Ha HJ; College of Pharmacy, Chung-Ang University, Dongjak-gu, Seoul, 06974, Republic of Korea.
Kang YJ; College of Pharmacy, Chung-Ang University, Dongjak-gu, Seoul, 06974, Republic of Korea.
Sung JH; College of Pharmacy, Chung-Ang University, Dongjak-gu, Seoul, 06974, Republic of Korea.
Hwang J; Research Unit of Cryogenic Novel Material, Korea Polar Research Institute, Incheon, 21990, Republic of Korea; Department of Polar Sciences, University of Science and Technology, Incheon, 21990, Republic of Korea.
Lee MJ; Research Unit of Cryogenic Novel Material, Korea Polar Research Institute, Incheon, 21990, Republic of Korea.
Lee JH; Research Unit of Cryogenic Novel Material, Korea Polar Research Institute, Incheon, 21990, Republic of Korea; Department of Polar Sciences, University of Science and Technology, Incheon, 21990, Republic of Korea. Electronic address: .
Park HH; College of Pharmacy, Chung-Ang University, Dongjak-gu, Seoul, 06974, Republic of Korea. Electronic address: .
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Źródło:
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Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2021 Dec 31; Vol. 585, pp. 48-54. Date of Electronic Publication: 2021 Nov 11.
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Typ publikacji:
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Journal Article; Research Support, Non-U.S. Gov't
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Język:
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English
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Imprint Name(s):
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Publication: <2002- >: San Diego, CA : Elsevier
Original Publication: New York, Academic Press.
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MeSH Terms:
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Catalytic Domain*
Protein Conformation*
Bacterial Proteins/*chemistry
Paenibacillus/*enzymology
Triose-Phosphate Isomerase/*chemistry
Amino Acids/genetics ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Binding Sites/genetics ; Crystallography, X-Ray ; Metals/chemistry ; Metals/metabolism ; Models, Molecular ; Paenibacillus/genetics ; Triose-Phosphate Isomerase/genetics ; Triose-Phosphate Isomerase/metabolism
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Contributed Indexing:
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Keywords: Cold adaptation; Glucose isomerase; Paenibacillus; Psychrophilic bacteria; Sugar isomerase; Xylose isomerase
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Substance Nomenclature:
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0 (Amino Acids)
0 (Bacterial Proteins)
0 (Metals)
EC 5.3.1.1 (Triose-Phosphate Isomerase)
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Entry Date(s):
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Date Created: 20211116 Date Completed: 20220103 Latest Revision: 20220103
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Update Code:
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20240105
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DOI:
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10.1016/j.bbrc.2021.11.026
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PMID:
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34784551
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Sugar isomerases (SIs) catalyze the reversible conversion of aldoses to ketoses. A novel putative SI gene has been identified from the genome sequence information on the psychrophilic bacterium Paenibacillus sp. R4. Here, we report the crystal structure of the putative SI from Paenibacillus sp. R4 (PbSI) at 2.98 Å resolution. It was found that the overall structure of PbSI adopts the triose-phosphate isomerase (TIM) barrel fold. PbSI was also identified to have two heterogeneous metal ions as its cofactors at the active site in the TIM barrel, one of which was confirmed as a Zn ion through X-ray anomalous scattering and inductively coupled plasma mass spectrometry analysis. Structural comparison with homologous SI proteins from mesophiles, hyperthermophiles, and a psychrophile revealed that key residues in the active site are well conserved and that dimeric PbSI is devoid of the extended C-terminal region, which tetrameric SIs commonly have. Our results provide novel structural information on the cold-adaptable SI, including information on the metal composition in the active site.
Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(Copyright © 2021 Elsevier Inc. All rights reserved.)