D
Dong Hae Shin
Researcher at UPRRP College of Natural Sciences
Publications - 13
Citations - 1056
Dong Hae Shin is an academic researcher from UPRRP College of Natural Sciences. The author has contributed to research in topics: Protein structure & Catalytic triad. The author has an hindex of 9, co-authored 11 publications receiving 1003 citations. Previous affiliations of Dong Hae Shin include Korea Research Institute of Bioscience and Biotechnology & Seoul National University.
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The crystal structure of a triacylglycerol lipase from Pseudomonas cepacia reveals a highly open conformation in the absence of a bound inhibitor.
TL;DR: The crystal structure of a triacylglycerol lipase from Pseudomonas cepacia (PcL) in the absence of a bound inhibitor using X-ray crystallography suggests that this enzyme shares the same mechanisms of catalysis and interfacial activation as other lipases.
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High-resolution crystal structure of the non-specific lipid-transfer protein from maize seedlings.
TL;DR: The fold of maize ns-LTP places it in a new category of all-alpha-type structure, first described for soybean hydrophobic protein, which is large enough to accommodate a long fatty acyl chain.
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Structural basis of non-specific lipid binding in maize lipid-transfer protein complexes revealed by high-resolution X-ray crystallography.
Gye Won Han,Jae Young Lee,Hyun Kyu Song,Changsoo Chang,Kyeongsik Min,Jinho Moon,Dong Hae Shin,Mary L. Kopka,Michael R. Sawaya,Hanna S. Yuan,Hanna S. Yuan,Thomas D. Kim,Jungwoo Choe,Dori Lim,Hee Jung Moon,Se Won Suh +15 more
TL;DR: The structural plasticity of the ligand binding cavity and the predominant involvement of non-specific van der Waals interactions with the hydrophobic tail of theligands provide a structural explanation for the non- specificity of maize nsLTP.
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Rice non-specific lipid transfer protein: the 1.6 A crystal structure in the unliganded state reveals a small hydrophobic cavity.
TL;DR: In this article, the authors describe the high-resolution X-ray structure of the non-specific lipid transfer protein (ns-LTP) from rice seeds in the unliganded state, and the model has been refined to a crystallographic R -factor of 0.186 for 8.0 to 1.6 A data (with F o > 2 σ F ).
Journal ArticleDOI
Crystal structure of carboxylesterase from Pseudomonas fluorescens, an α/β hydrolase with broad substrate specificity
Kyeong Kyu Kim,Hyun Kyu Song,Dong Hae Shin,Kwang Yeon Hwang,Senyon Choe,Ook Joon Yoo,Se Won Suh +6 more
TL;DR: The crystal structure of carboxylesterase from P. fluorescens has the α/β hydrolase fold and the Ser‐His‐Asp catalytic triad, and it may be these extra structural elements, not seen in other esterases, that account for the inability of carboxeserase to hydrolyze long chain fatty acids.