scholarly journals Crystal structure ofd-stereospecific amidohydrolase fromStreptomycessp. 82F2 - insight into the structural factors for substrate specificity

FEBS Journal ◽  
2015 ◽  
Vol 283 (2) ◽  
pp. 337-349 ◽  
Author(s):  
Jiro Arima ◽  
Kana Shimone ◽  
Kazusa Miyatani ◽  
Yuka Tsunehara ◽  
Yoshitaka Isoda ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Substrate Specificity ◽  
Structural Factors ◽  
Insight Into

scholarly journals The crystal structure of mycobacterial epoxide hydrolase A

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Eike C. Schulz ◽  
Sara R. Henderson ◽  
Boris Illarionov ◽  
Thomas Crosskey ◽  
Stacey M. Southall ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Substrate Specificity ◽  
Drug Targets ◽  
Epoxide Hydrolase ◽  
Sequence Similarity ◽  
Structural Similarity ◽  
High Sequence Similarity ◽  
High Structural Similarity ◽  
Potential Drug Targets ◽  
Insight Into

Abstract The human pathogen Mycobacterium tuberculosis is the causative agent of tuberculosis resulting in over 1 million fatalities every year, despite decades of research into the development of new anti-TB compounds. Unlike most other organisms M. tuberculosis has six putative genes for epoxide hydrolases (EH) of the α/β-hydrolase family with little known about their individual substrates, suggesting functional significance for these genes to the organism. Due to their role in detoxification, M. tuberculosis EH’s have been identified as potential drug targets. Here, we demonstrate epoxide hydrolase activity of M. thermoresistibile epoxide hydrolase A (Mth-EphA) and report its crystal structure in complex with the inhibitor 1,3-diphenylurea at 2.0 Å resolution. Mth-EphA displays high sequence similarity to its orthologue from M. tuberculosis and generally high structural similarity to α/β-hydrolase EHs. The structure of the inhibitor bound complex reveals the geometry of the catalytic residues and the conformation of the inhibitor. Comparison to other EHs from mycobacteria allows insight into the active site plasticity with respect to substrate specificity. We speculate that mycobacterial EHs may have a narrow substrate specificity providing a potential explanation for the genetic repertoire of epoxide hydrolase genes in M. tuberculosis.

scholarly journals Correction: Crystal Structure of Human Myotubularin-Related Protein 1 Provides Insight into the Structural Basis of Substrate Specificity

PLoS ONE ◽  
2018 ◽  
Vol 13 (1) ◽  
pp. e0190844
Author(s):  
Seoung Min Bong ◽  
Kka-bi Son ◽  
Seung-Won Yang ◽  
Jae-Won Park ◽  
Jea-Won Cho ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Substrate Specificity ◽  
Structural Basis ◽  
Related Protein ◽  
Insight Into

scholarly journals The crystal structure and insight into the substrate specificity of the α-L rhamnosidase RHA-P from Novosphingobium sp. PP1Y

2020 ◽  
Vol 679 ◽  
pp. 108189
Author(s):  
Brendan Terry ◽  
Joseph Ha ◽  
Federica De Lise ◽  
Francesca Mensitieri ◽  
Viviana Izzo ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Substrate Specificity ◽  
Insight Into

scholarly journals Correction to Crystal Structure of α-Galactosidase from Thermus thermophilus: Insight into Hexamer Assembly and Substrate Specificity

2020 ◽  
Vol 68 (30) ◽  
pp. 8091-8091
Author(s):  
Sheng-Chia Chen ◽  
Szu-Pei Wu ◽  
Yu-Yung Chang ◽  
Tzann-Shun Hwang ◽  
Tzong-Huei Lee ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Substrate Specificity ◽  
Thermus Thermophilus ◽  
Insight Into

scholarly journals Crystal Structure of Human Myotubularin-Related Protein 1 Provides Insight into the Structural Basis of Substrate Specificity

PLoS ONE ◽  
2016 ◽  
Vol 11 (3) ◽  
pp. e0152611 ◽  
Author(s):  
Seoung Min Bong ◽  
Kka-bi Son ◽  
Seung-Won Yang ◽  
Jae-Won Park ◽  
Jea-Won Cho ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Substrate Specificity ◽  
Structural Basis ◽  
Related Protein ◽  
Insight Into

Crystal Structure of α-Galactosidase from Thermus thermophilus: Insight into Hexamer Assembly and Substrate Specificity

2020 ◽  
Vol 68 (22) ◽  
pp. 6161-6169
Author(s):  
Sheng-Chia Chen ◽  
Szu-Pei Wu ◽  
Yu-Yung Chang ◽  
Tzann-Shun Hwang ◽  
Tzong-Huei Lee ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Substrate Specificity ◽  
Thermus Thermophilus ◽  
Insight Into

Crystal structure of KBSi3O8 isostructural with danburite

1993 ◽  
Vol 57 (386) ◽  
pp. 157-164 ◽  
Author(s):  
Mitsuyoshi Kimata
Keyword(s):  
Crystal Structure ◽  
Direct Method ◽  
Crystal Chemical ◽  
Chemical Formula ◽  
Crystal Chemical Formula ◽  
3 Dimensional ◽  
Tetrahedral Sites ◽  
Structural Types ◽  
Coupled Substitution ◽  
Insight Into

AbstractThe crystal structure of KBSi3O8 (orthorhombic, Pnam, with a = 8.683(1), b = 9.253(1), c = 8.272(1) Å,, V = 664.4(1) Å3, Z = 4) has been determined by the direct method applied to 3- dimensional rcflection data. The structure of a microcrystal with the dimensions 20 × 29 × 37 μm was refined to an unweightcd residual of R = 0.031 using 386 non-zero structure amplitudes. KBSi3O8 adopts a structure essentially different from recdmergneritc NaBSi3O8, with the low albite (NaAlSi3O8) structure, and isotypic with danburite CaB2Si2Os which has the same topology as paracelsian BaAl2Si2O8. The chenfical relationship between this sample and danburitc gives insight into a new coupled substitution; K+ + Si4+ = Ca2+ + B3+ in the extraframework and tetrahedral sites. The present occupancy refinement revealed partial disordering of B and Si atoms which jointly reside in two kinds of general equivalent points, T(1) and T(2) sites. Thus the expanded crystal-chemical formula can be written in the form K(B0.44Si0.56)2(B0.06Si0.94)2O8The systematic trend among crystalline compounds with the M+T3+T4+3O8 formula suggests that they exist in one of four structural types; the feldspar structures with T3+/T4+ ordered and/or disordered forms, and the paracelsian and the hollandite structures.

Sign in / Sign up

Export Citation Format

Share Document