scholarly journals Crystal structure of CobK reveals strand-swapping between Rossmann-fold domains and molecular basis of the reduced precorrin product trap

2015 ◽  
Vol 5 (1) ◽  
Author(s):  
Shuang Gu ◽  
Oleksandr Sushko ◽  
Evelyne Deery ◽  
Martin J. Warren ◽  
Richard W. Pickersgill
Keyword(s):  
Crystal Structure ◽  
Molecular Basis ◽  
Rossmann Fold

scholarly journals Structural analysis of human dual-specificity phosphatase 22 complexed with a phosphotyrosine-like substrate

2015 ◽  
Vol 71 (2) ◽  
pp. 199-205 ◽  
Author(s):  
George T. Lountos ◽  
Scott Cherry ◽  
Joseph E. Tropea ◽  
David S. Waugh
Keyword(s):  
Crystal Structure ◽  
Structural Analysis ◽  
Phosphatase Activity ◽  
Small Molecule ◽  
Molecular Basis ◽  
Protein Tyrosine Phosphatases ◽  
Simple Method ◽  
Dual Specificity Phosphatase ◽  
Dual Specificity ◽  
Nitrophenyl Phosphate

4-Nitrophenyl phosphate (p-nitrophenyl phosphate, pNPP) is widely used as a small molecule phosphotyrosine-like substrate in activity assays for protein tyrosine phosphatases. It is a colorless substrate that upon hydrolysis is converted to a yellow 4-nitrophenolate ion that can be monitored by absorbance at 405 nm. Therefore, the pNPP assay has been widely adopted as a quick and simple method to assess phosphatase activity and is also commonly used in assays to screen for inhibitors. Here, the first crystal structure is presented of a dual-specificity phosphatase, human dual-specificity phosphatase 22 (DUSP22), in complex with pNPP. The structure illuminates the molecular basis for substrate binding and may also facilitate the structure-assisted development of DUSP22 inhibitors.

The Crystal Structure of the C-Terminal DAP5/p97 Domain Sheds Light on the Molecular Basis for Its Processing by Caspase Cleavage

2008 ◽  
Vol 383 (3) ◽  
pp. 539-548 ◽  
Author(s):  
Noa Liberman ◽  
Orly Dym ◽  
Tamar Unger ◽  
Shira Albeck ◽  
Yoav Peleg ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Molecular Basis ◽  
Caspase Cleavage

scholarly journals Crystal structure and interactions of the Tof1–Csm3 (Timeless–Tipin) fork protection complex

2020 ◽  
Vol 48 (12) ◽  
pp. 6996-7004 ◽  
Author(s):  
Daniel B Grabarczyk
Keyword(s):  
Crystal Structure ◽  
Circadian Rhythm ◽  
Dna Replication ◽  
Binding Site ◽  
Molecular Basis ◽  
Replication Forks ◽  
Repeat Structure ◽  
Chaetomium Thermophilum ◽  
Fork Protection Complex ◽  
Human Orthologue

Abstract The Tof1–Csm3 fork protection complex has a central role in the replisome—it promotes the progression of DNA replication forks and protects them when they stall, while also enabling cohesion establishment and checkpoint responses. Here, I present the crystal structure of the Tof1–Csm3 complex from Chaetomium thermophilum at 3.1 Å resolution. The structure reveals that both proteins together form an extended alpha helical repeat structure, which suggests a mechanical or scaffolding role for the complex. Expanding on this idea, I characterize a DNA interacting region and a cancer-associated Mrc1 binding site. This study provides the molecular basis for understanding the functions of the Tof1–Csm3 complex, its human orthologue the Timeless–Tipin complex and additionally the Drosophila circadian rhythm protein Timeless.

Crystal structure of basal pilin SpaE reveals the molecular basis of its incorporation in the lactobacillar SpaFED pilus

2019 ◽  
Vol 207 (1) ◽  
pp. 74-84 ◽  
Author(s):  
Abhin Kumar Megta ◽  
Arjun K. Mishra ◽  
Airi Palva ◽  
Ingemar von Ossowski ◽  
Vengadesan Krishnan
Keyword(s):  
Crystal Structure ◽  
Molecular Basis

scholarly journals Irreversible inactivation of ISG15 by a viral leader protease enables alternative infection detection strategies

2018 ◽  
Vol 115 (10) ◽  
pp. 2371-2376 ◽  
Author(s):  
Kirby N. Swatek ◽  
Martina Aumayr ◽  
Jonathan N. Pruneda ◽  
Linda J. Visser ◽  
Stephen Berryman ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Viral Infection ◽  
Posttranslational Modifications ◽  
Molecular Basis ◽  
Foot And Mouth Disease ◽  
Peptide Bond ◽  
Infection Detection ◽  
Mouth Disease Virus ◽  
Host Signaling ◽  
Detection Strategies

In response to viral infection, cells mount a potent inflammatory response that relies on ISG15 and ubiquitin posttranslational modifications. Many viruses use deubiquitinases and deISGylases that reverse these modifications and antagonize host signaling processes. We here reveal that the leader protease, Lbpro, from foot-and-mouth disease virus (FMDV) targets ISG15 and to a lesser extent, ubiquitin in an unprecedented manner. Unlike canonical deISGylases that hydrolyze the isopeptide linkage after the C-terminal GlyGly motif, Lbpro cleaves the peptide bond preceding the GlyGly motif. Consequently, the GlyGly dipeptide remains attached to the substrate Lys, and cleaved ISG15 is rendered incompetent for reconjugation. A crystal structure of Lbpro bound to an engineered ISG15 suicide probe revealed the molecular basis for ISG15 proteolysis. Importantly, anti-GlyGly antibodies, developed for ubiquitin proteomics, are able to detect Lbpro cleavage products during viral infection. This opens avenues for infection detection of FMDV based on an immutable, host-derived epitope.

Sign in / Sign up

Export Citation Format

Share Document