protein structure – Page 2 – Lightsources.org

ALS passes the 7000-protein milestone

2018/05/302018/06/11

The eight structural biology beamlines at the ALS have now collectively deposited over 7000 proteins into the Protein Data Bank (PDB), a worldwide, open-access repository of protein structures. The 7000th ALS protein structure (entry no. 6C7C) is an enzyme from Mycobacterium ulcerans (strain Agy99), solved with data from Beamline 5.0.2. This bacterium produces a toxin that eats away at skin tissue, causing what’s known as Buruli ulcers (Google at your own risk!). The bacterium is antibiotic-resistant, and treatment involves the surgical removal of infected tissues, including amputation.

The enzyme structure was solved by a group from the Seattle Structural Genomics Center for Infectious Disease (SSGID), whose mission is to obtain crystal structures of potential drug targets on the priority pathogen list of the National Institute of Allergy and Infectious Diseases (NIAID). As of May 2018, SSGCID has deposited 1090 structures in the PDB, with data for more than a quarter of those collected at ALS beamlines.

Image: PDB 6C7C: Enoyl-CoA hydratase, an enzyme from M. ulcerans (strain Agy99).

With help from a few friends

2018/02/152018/02/19

Researchers discover the precise make-up of a molecular chaperone complex

A complex made up of three proteins, Hsp90, Sgt1, and Rar1, is thought to stabilise an important immune protein known as nucleotide-binding domain and leucine-rich repeat containing protein. While the structure of the Sgt1-Hsp90-Rar1 protein is known, the stoichiometry of the complex has remained elusive. In a paper published in Frontiers in Molecular Biosciences, Dr Chrisostomos Prodromou of the University of Sussex and Dr Minghao Zhang of the University of Oxford worked with Professor Giuliano Siligardi at the Circular Dichroism beamline (B23) at Diamond Light Source to clarify the detailed make-up of the complex. Using synchrotron radiation circular dichroism, they revealed that it consists of an Hsp90 dimer, two Sgt1 molecules, and a single Rar1 molecule. The stoichiometry of the full complex potentially allows two NLR molecules to bind, a finding which may open avenues of research into how these proteins form dimers.

Figure: (extract) The structure of the Sgt1-Hsp90-Rar1 complex with an Hsp90 dimer, two Sgt1 molecules, and a single Rar1. Entire image here.

Crystallographers identify 1,000 protein structures

2017/11/232018/04/25

The Canadian Light Source is celebrating two milestones reached by scientists who have conducted research at the national facility at the University of Saskatchewan.

Scientists have solved 1,000 protein structures using data collected at CLS’s CMCF beamlines. These have been added to the Protein Data Bank – a collection of structures solved by researchers globally. Researchers have also published 500 scientific papers based on their work using the crystallography beamlines.

Proteins are the building blocks of life and are described as the body’s workhorses. The body is made of trillions of cells. Cells produce proteins, which do the work of breaking down food, sending messages to other cells, and fighting bacteria, viruses and parasites. The discoveries at the CLS range from how the malaria parasite invades red blood cells to why superbugs are resistant to certain antibiotics and how parkin protein mutations result in some types of Parkinson’s disease. Understanding how these and other such proteins work can potentially save millions of lives.

Image: PDB ID: 6B0S