scholarly journals High Resolution Crystal Structure of the Catalytic Domain of ADAMTS-5 (Aggrecanase-2)

2007 ◽  
Vol 283 (3) ◽  
pp. 1501-1507 ◽  
Author(s):  
Huey-Sheng Shieh ◽  
Karl J. Mathis ◽  
Jennifer M. Williams ◽  
Robert L. Hills ◽  
Joe F. Wiese ◽  
...  
Keyword(s):  
Crystal Structure ◽  
High Resolution ◽  
Catalytic Domain ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Direct Role ◽  
Three Dimensional Structure ◽  
High Resolution Structure ◽  
A Disintegrin And Metalloproteinase ◽  
Resolution Structure

Aggrecanase-2 (a disintegrin and metalloproteinase with thrombospondin motifs-5 (ADAMTS-5)), a member of the ADAMTS protein family, is critically involved in arthritic diseases because of its direct role in cleaving the cartilage component aggrecan. The catalytic domain of aggrecanase-2 has been refolded, purified, and crystallized, and its three-dimensional structure determined to 1.4Å resolution in the presence of an inhibitor. A high resolution structure of an ADAMTS/aggrecanase protein provides an opportunity for the development of therapeutics to treat osteoarthritis.

scholarly journals Three-dimensional structure of the catalytic domain of chitinase Al from Bacillus circulars WL-12 at a very high resolution

1999 ◽  
Vol 75 (9) ◽  
pp. 269-274 ◽  
Author(s):  
Takuo MATSUMOTO ◽  
Takamasa NONAKA ◽  
Masayuki HASHIMOTO ◽  
Takeshi WATANABE ◽  
Yukio MITSUI
Keyword(s):  
High Resolution ◽  
Catalytic Domain ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Three Dimensional Structure ◽  
Very High

scholarly journals High-resolution structure of viruses from random diffraction snapshots

2014 ◽  
Vol 369 (1647) ◽  
pp. 20130326 ◽  
Author(s):  
A. Hosseinizadeh ◽  
P. Schwander ◽  
A. Dashti ◽  
R. Fung ◽  
R. M. D'Souza ◽  
...  
Keyword(s):  
High Resolution ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Tobacco Necrosis Virus ◽  
Bayesian Approaches ◽  
X Ray ◽  
Three Dimensional Structure ◽  
Nano Crystalline ◽  
High Resolution Structure ◽  
Biological Entities

The advent of the X-ray free-electron laser (XFEL) has made it possible to record diffraction snapshots of biological entities injected into the X-ray beam before the onset of radiation damage. Algorithmic means must then be used to determine the snapshot orientations and thence the three-dimensional structure of the object. Existing Bayesian approaches are limited in reconstruction resolution typically to 1/10 of the object diameter, with the computational expense increasing as the eighth power of the ratio of diameter to resolution. We present an approach capable of exploiting object symmetries to recover three-dimensional structure to high resolution, and thus reconstruct the structure of the satellite tobacco necrosis virus to atomic level. Our approach offers the highest reconstruction resolution for XFEL snapshots to date and provides a potentially powerful alternative route for analysis of data from crystalline and nano-crystalline objects.

The first crystal structure of the peptidase domain of the U32 peptidase family

2015 ◽  
Vol 71 (12) ◽  
pp. 2505-2512 ◽  
Author(s):  
Magdalena Schacherl ◽  
Angelika A. M. Montada ◽  
Elena Brunstein ◽  
Ulrich Baumann
Keyword(s):  
Crystal Structure ◽  
Catalytic Mechanism ◽  
Quaternary Structure ◽  
Catalytic Domain ◽  
Three Dimensional ◽  
Zinc Ion ◽  
Crystal Structure Analysis ◽  
Dimensional Structure ◽  
Sequence Motifs ◽  
Conserved Sequence

The U32 family is a collection of over 2500 annotated peptidases in the MEROPS database with unknown catalytic mechanism. They mainly occur in bacteria and archaea, but a few representatives have also been identified in eukarya. Many of the U32 members have been linked to pathogenicity, such as proteins fromHelicobacterandSalmonella. The first crystal structure analysis of a U32 catalytic domain fromMethanopyrus kandleri(genemk0906) reveals a modified (βα)8TIM-barrel fold with some unique features. The connecting segment between strands β7 and β8 is extended and helix α7 is located on top of the C-terminal end of the barrel body. The protein exhibits a dimeric quaternary structure in which a zinc ion is symmetrically bound by histidine and cysteine side chains from both monomers. These residues reside in conserved sequence motifs. No typical proteolytic motifs are discernible in the three-dimensional structure, and biochemical assays failed to demonstrate proteolytic activity. A tunnel in which an acetate ion is bound is located in the C-terminal part of the β-barrel. Two hydrophobic grooves lead to a tunnel at the C-terminal end of the barrel in which an acetate ion is bound. One of the grooves binds to aStrep-Tag II of another dimer in the crystal lattice. Thus, these grooves may be binding sites for hydrophobic peptides or other ligands.

scholarly journals Crystal structure of 3-deoxy-3-nitromethyl-1,2;5,6-di-O-isopropylidene-α-D-allofuranose

2016 ◽  
Vol 72 (3) ◽  
pp. 314-317
Author(s):  
Jevgeņija Lugiņina ◽  
Vitālijs Rjabovs ◽  
Dmitrijs Stepanovs
Keyword(s):  
Crystal Structure ◽  
Hydrogen Bonds ◽  
Title Compound ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Three Dimensional Structure ◽  
Compound C

The title compound, C13H21NO7{systematic name: (3aR,5S,6R,6aR)-5-[(R)-2,2-dimethyl-1,3-dioxolan-4-yl]-2,2-dimethyl-6-(nitromethyl)tetrahydrofuro[2,3-d][1,3]dioxole}, consists of a substituted 2,2-dimethyltetrahydrofuro[2,3-d][1,3]dioxolane skeleton. The furanose ringAadopts aoT4conformation. The fused dioxolane ringBand the substituent dioxolane ringCalso have twisted conformations. There are no strong hydrogen bonds in the crystal structure: only weak C—H...O contacts are present, which link the molecules to form a three-dimensional structure.

scholarly journals Crystal structure of trichlorido(4′-ferrocenyl-2,2′:6′,2′′-terpyridine-κ3N,N′,N′′)iridium(III) acetonitrile disolvate

2015 ◽  
Vol 71 (3) ◽  
pp. m69-m70 ◽  
Author(s):  
Bambar Davaasuren ◽  
Harihara Padhy ◽  
Alexander Rothenberger
Keyword(s):  
Crystal Structure ◽  
Title Compound ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Three Dimensional Structure ◽  
Ferrocenyl Group ◽  
Distorted Octahedral ◽  
Chloride Ligands ◽  
Solvent Molecules

In the title compound, [FeIr(C5H5)(C20H14N3)Cl3]·2CH3CN, the central IrIIIatom is sixfold coordinated by three chloride ligands and three terpyridine N atoms in a slightly distorted octahedral fashion. The terpyridine ligand is functionalized at the 4′-position with a ferrocenyl group, the latter being in an eclipsed conformation. In the crystal, molecules are stacked in rows parallel to [001], with the acetonitrile solvent molecules situated between the rows. An extensive network of intra- and intermolecular C—H...Cl interactions is present, stabilizing the three-dimensional structure.

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