scholarly journals High resolution crystal structure of the catalytic domain of MCR-1

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Guixing Ma ◽  
Yifan Zhu ◽  
Zhicheng Yu ◽  
Ashfaq Ahmad ◽  
Hongmin Zhang
Keyword(s):  
Crystal Structure ◽  
High Resolution ◽  
Catalytic Domain

scholarly journals 1.12 Å resolution crystal structure of the catalytic domain of the plasmid-mediated colistin resistance determinant MCR-2

2017 ◽  
Vol 73 (8) ◽  
pp. 443-449 ◽  
Author(s):  
Katie Coates ◽  
Timothy R. Walsh ◽  
James Spencer ◽  
Philip Hinchliffe
Keyword(s):  
Crystal Structure ◽  
Amino Acids ◽  
High Resolution ◽  
Active Site ◽  
Catalytic Domain ◽  
Resistance Determinant ◽  
Mechanistic Studies ◽  
Colistin Resistance ◽  
Gram Negative ◽  
Starting Model

MCR-2 confers resistance to colistin, a `last-line' antibiotic against extensively resistant Gram-negative pathogens. It is a plasmid-encoded phosphoethanolamine transferase that is closely related to MCR-1. To understand the diversity in the MCR family, the 1.12 Å resolution crystal structure of the catalytic domain of MCR-2 was determined. Variable amino acids are located distant from both the di-zinc active site and the membrane-proximal face. The exceptionally high resolution will provide an accurate starting model for further mechanistic studies.

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.

High-resolution crystal structure of the catalytic domain of human dual-specificity phosphatase 26

2013 ◽  
Vol 69 (6) ◽  
pp. 1160-1170 ◽  
Author(s):  
Eun-Young Won ◽  
Yong Xie ◽  
Chie Takemoto ◽  
Lirong Chen ◽  
Zhi-Jie Liu ◽  
...  
Keyword(s):  
Crystal Structure ◽  
High Resolution ◽  
Catalytic Domain ◽  
Dual Specificity Phosphatase ◽  
Dual Specificity

High resolution STEM imaging study on high Tc superconductor YBa2CuaO7-x

1988 ◽  
Vol 46 ◽  
pp. 882-883
Author(s):  
H.-J. Ou ◽  
J. M. Cowley
Keyword(s):  
Crystal Structure ◽  
High Resolution ◽  
Grain Boundary ◽  
Strong Field ◽  
Imaging Study ◽  
Structure Defects ◽  
High Tc ◽  
High Tc Superconductor ◽  
Diffraction Patterns ◽  
Lattice Planes

Using the dedicate VG-HB5 STEM microscope, the crystal structure of high Tc superconductor of YBa2Cu3O7-x has been studied via high resolution STEM (HRSTEM) imaging and nanobeam (∽3A) diffraction patterns. Figure 1(a) and 2(a) illustrate the HRSTEM image taken at 10' times magnification along [001] direction and [100] direction, respectively. In figure 1(a), a grain boundary with strong field contrast is seen between two crystal regions A and B. The grain boundary appears to be parallel to a (110) plane, although it is not possible to determine [100] and [001] axes as it is in other regions which contain twin planes [3]. Following the horizontal lattice lines, from left to right across the grain boundary, a lattice bending of ∽4° is noticed. Three extra lattice planes, indicated by arrows, were found to terminate at the grain boundary and form dislocations. It is believed that due to different chemical composition, such structure defects occur during crystal growth. No bending is observed along the vertical lattice lines.

Perovskite Solar Cells: Crystal Structure and Interface Architecture with High Resolution TEM Observations

2017 ◽  
Author(s):  
Satoshi Uchida ◽  
Tae Woong Kim ◽  
Ludmila Cojocaru ◽  
Takashi Kondo ◽  
Hiroshi Segawa
Keyword(s):  
Crystal Structure ◽  
Solar Cells ◽  
High Resolution ◽  
Perovskite Solar Cells ◽  
High Resolution Tem

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.

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