Crystal structure of the SPRY domain-containing protein 7 reveals unique structural features

2020 ◽  
Vol 531 (3) ◽  
pp. 350-356
Author(s):  
Jinjin Yang ◽  
Xueyan Guan ◽  
Danting Zhang ◽  
Panqi Zhao ◽  
Shujun Guo ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Structural Features ◽  
Spry Domain

scholarly journals The crystal structure of the first ether solvate of hexaphenyldistannane [(Ph3Sn)2 • 2 THF]

2020 ◽  
Vol 43 (1) ◽  
pp. 1-6 ◽  
Author(s):  
Jonathan O. Bauer
Keyword(s):  
Crystal Structure ◽  
Inclusion Compounds ◽  
Molecular Crystal ◽  
Structural Features ◽  
Structural Investigations ◽  
Crystal Solvates

AbstractStructural investigations of molecular crystal solvates can provide important information for the targeted crystallization of particular inclusion compounds. Here, the crystal structure of the first ether solvate of hexaphenyldistannane [(Ph3Sn)2 • 2 THF] is reported. Structural features in terms of host-guest interactions and in the context of the previously reported polymorphs and solvates of (Ph3Sn)2 are discussed.

Crystal structure of PRY-SPRY domain of human TRIM72

2009 ◽  
pp. NA-NA ◽  
Author(s):  
Eun Young Park ◽  
Oh-Bong Kwon ◽  
Byung-Cheon Jeong ◽  
Jae-Sung Yi ◽  
Chang Seok Lee ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Spry Domain

Structural insights into dihydroxylation of terephthalate, a product of polyethylene terephthalate degradation

2022 ◽  
Author(s):  
Jai Krishna Mahto ◽  
Neetu Neetu ◽  
Monica Sharma ◽  
Monika Dubey ◽  
Bhanu Prakash Vellanki ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Substrate Specificity ◽  
Polyethylene Terephthalate ◽  
Active Site ◽  
Catalytic Domain ◽  
Structural Features ◽  
Comamonas Testosteroni ◽  
Plastic Pollution ◽  
Microbial Utilization ◽  
Steady State Kinetics

Biodegradation of terephthalate (TPA) is a highly desired catabolic process for the bacterial utilization of this Polyethylene terephthalate (PET) depolymerization product, but to date, the structure of terephthalate dioxygenase (TPDO), a Rieske oxygenase (RO) that catalyzes the dihydroxylation of TPA to a cis -diol is unavailable. In this study, we characterized the steady-state kinetics and first crystal structure of TPDO from Comamonas testosteroni KF1 (TPDO KF1 ). The TPDO KF1 exhibited the substrate specificity for TPA ( k cat / K m = 57 ± 9 mM −1 s −1 ). The TPDO KF1 structure harbors characteristics RO features as well as a unique catalytic domain that rationalizes the enzyme’s function. The docking and mutagenesis studies reveal that its substrate specificity to TPA is mediated by Arg309 and Arg390 residues, two residues positioned on opposite faces of the active site. Additionally, residue Gln300 is also proven to be crucial for the activity, its substitution to alanine decreases the activity ( k cat ) by 80%. Together, this study delineates the structural features that dictate the substrate recognition and specificity of TPDO. Importance The global plastic pollution has become the most pressing environmental issue. Recent studies on enzymes depolymerizing polyethylene terephthalate plastic into terephthalate (TPA) show some potential in tackling this. Microbial utilization of this released product, TPA is an emerging and promising strategy for waste-to-value creation. Research from the last decade has discovered terephthalate dioxygenase (TPDO), as being responsible for initiating the enzymatic degradation of TPA in a few Gram-negative and Gram-positive bacteria. Here, we have determined the crystal structure of TPDO from Comamonas testosteroni KF1 and revealed that it possesses a unique catalytic domain featuring two basic residues in the active site to recognize TPA. Biochemical and mutagenesis studies demonstrated the crucial residues responsible for the substrate specificity of this enzyme.

Peroxisomal multifunctional enzyme type 2 from the fruitfly: dehydrogenase and hydratase act as separate entities, as revealed by structure and kinetics

2011 ◽  
Vol 435 (3) ◽  
pp. 771-781 ◽  
Author(s):  
Tatu J. K. Haataja ◽  
M. Kristian Koski ◽  
J. Kalervo Hiltunen ◽  
Tuomo Glumoff
Keyword(s):  
Crystal Structure ◽  
Saccharomyces Cerevisiae ◽  
Drosophila Melanogaster ◽  
Structural Features ◽  
Full Length ◽  
Multifunctional Enzyme ◽  
Domain Composition ◽  
Substrate Channelling

All of the peroxisomal β-oxidation pathways characterized thus far house at least one MFE (multifunctional enzyme) catalysing two out of four reactions of the spiral. MFE type 2 proteins from various species display great variation in domain composition and predicted substrate preference. The gene CG3415 encodes for Drosophila melanogaster MFE-2 (DmMFE-2), complements the Saccharomyces cerevisiae MFE-2 deletion strain, and the recombinant protein displays both MFE-2 enzymatic activities in vitro. The resolved crystal structure is the first one for a full-length MFE-2 revealing the assembly of domains, and the data can also be transferred to structure–function studies for other MFE-2 proteins. The structure explains the necessity of dimerization. The lack of substrate channelling is proposed based on both the structural features, as well as by the fact that hydration and dehydrogenation activities of MFE-2, if produced as separate enzymes, are equally efficient in catalysis as the full-length MFE-2.

Crystal Structure of Human Dual-Specificity Tyrosine-Regulated Kinase 3 Reveals New Structural Features and Insights into its Auto-phosphorylation

2018 ◽  
Vol 430 (10) ◽  
pp. 1521-1530 ◽  
Author(s):  
Kuglae Kim ◽  
Jeong Seok Cha ◽  
Yong-Soon Cho ◽  
Hoyoung Kim ◽  
Nienping Chang ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Structural Features ◽  
Dual Specificity

The alternative oxidases: simple oxidoreductase proteins with complex functions

2013 ◽  
Vol 41 (5) ◽  
pp. 1305-1311 ◽  
Author(s):  
Luke Young ◽  
Tomoo Shiba ◽  
Shigeharu Harada ◽  
Kiyoshi Kita ◽  
Mary S. Albury ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Electron Transport ◽  
Alternative Oxidase ◽  
Structural Features ◽  
Transport Proteins ◽  
Integral Membrane Proteins ◽  
Complex Functions ◽  
Membrane Bound ◽  
Iron Carboxylate ◽  
Electron Transport Proteins

The alternative oxidases are membrane-bound monotopic terminal electron transport proteins found in all plants and in some agrochemically important fungi and parasites including Trypansoma brucei, which is the causative agent of trypanosomiasis. They are integral membrane proteins and reduce oxygen to water in a four electron process. The recent elucidation of the crystal structure of the trypanosomal alternative oxidase at 2.85 Å (1 Å=0.1 nm) has revealed salient structural features necessary for its function. In the present review we compare the primary and secondary ligation spheres of the alternative oxidases with other di-iron carboxylate proteins and propose a mechanism for the reduction of oxygen to water.

New Ternary Phosphide La7Pd17P12: Preparation and Crystal Structure

2002 ◽  
Vol 57 (12) ◽  
pp. 1409-1413 ◽  
Author(s):  
S. Budnyk ◽  
Yu. Prots ◽  
Yu. Kuz’ma ◽  
Yu. Grin
Keyword(s):  
Crystal Structure ◽  
Temperature Region ◽  
Large Family ◽  
Structural Features ◽  
Structural Motif ◽  
Crystal Data ◽  
Monoclinic Structure ◽  
X Ray ◽  
Data Space ◽  
Metal Ratio

The title compound was prepared from elements by sintering in the temperature region between 1073 and 1473 K. The monoclinic structure of La7Pd17P12 was solved and refined from X-ray single crystal data: space group C2/m, a = 24.519(1), b = 4.0859(5), c = 13.6106(8)Å , β = 112.129(3)°, Z = 2, RF = 0.025 for 1065 unique of 4877 measured reflections and 112 refined parameters. Main structural motif of the new phosphide are condensed blocks of trigonal prisms around phosphorus atoms connected to infinite chains via lanthanum atoms. The structural features of La7Pd17P12 are discussed in comparison with some representatives of a large family of structures with metal / non-metal ratio close to 2 : 1.

Structural Features of Nominally Pure Lithium Niobate Crystals Grown from Boron-Doped Charge

2020 ◽  
Vol 312 ◽  
pp. 128-133
Author(s):  
Nikolay Sidorov ◽  
Roman Titov ◽  
Natalya A. Teplyakova ◽  
Mikhail Palatnikov ◽  
Alexander Vjacheslavovich Syuy
Keyword(s):  
Crystal Structure ◽  
Lithium Niobate ◽  
Single Crystals ◽  
Czochralski Method ◽  
Structural Features ◽  
Structural Defects ◽  
Cation Sublattice ◽  
Structural Units ◽  
Boron Doped ◽  
Lithium Niobate Crystals

The features of the structure of single crystals LiNbO3:B3+ (0.12 and 0.18 wt %) grown by the Czochralski method from the mixture of different genesis were studied. It was found that boron is able to incorporate into the crystal structure of lithium niobate in a trace amounts (~ 10–4–10–5 wt %), decreasing the concentration of structural defects NbLi. Thus, ordering of structural units of the cation sublattice of lithium niobate crystals grown from a congruent composition melt approach in that of stoichiometric crystals.

The Transition Metal-rich Orthophosphate Arrojadite with Special Structural Features

2010 ◽  
Vol 65 (12) ◽  
pp. 1427-1433 ◽  
Author(s):  
Christoph Kallfaß ◽  
Constantin Hoch ◽  
Hermann Schier ◽  
Arndt Simon ◽  
Helmut Schuber
Keyword(s):  
Crystal Structure ◽  
Transition Metal ◽  
Single Crystal ◽  
Structural Features ◽  
Nickel Plate ◽  
Single Crystal Diffraction ◽  
X Ray ◽  
Different Types ◽  
New Feature

The crystal structure of the transition metal-rich orthophosphate mineral arrojadite was reexamined, and the disorder phenomena were analyzed applying modern X-ray single-crystal diffraction and refinement methods on samples from Nickel Plate (USA) and Hagendorf (Germany). As a new feature of the arrojadite structure, two different types of channels oriented along [010] are described. The occupancy of the atomic positions inside these channels have been elucidated.

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