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PSI Structures of the Month

These images have appeared as PSI Structures of the Month.  To learn more about an image, click on its thumbnail in the gallery below.

Structure of the enolase yitF enzyme from Bacillus subtilis, a Gram positive bacterium commonly found in soil. Credit: New York Structural GenomiX ConsortiumX-ray structure of a new DNA repair enzyme superfamily representative from the human gastrointestinal bacterium Enterococcus faecalis. European scientists used this structure to generate homologous structures. Credit: Midwest Center for Structural GenomicsNMR solution structure of a plant protein that may function in host defense. This protein was expressed in a convenient and efficient wheat germ cell-free system. Credit: Center for Eukaryotic Structural GenomicsStructure of a magnesium transporter protein from an antibiotic-resistant bacterium found in the human gut. Credit:New York Structural GenomiX ConsortiumCrystal structure of Oligoendopeptidase F, a protein slicing enzyme from Bacillus stearothermophilus, a bacterium that can cause food products to spoil. The crystal was formed using a microfluidic capillary, a device that enables scientists to independently control the parameters for protein crystal nucleation and growth.This is the first structure of a protein derived from the metagenomic sequences collected during the Sorcerer II Global Ocean Sampling project. The crystal structure shows a barrel protein with a ferredoxin-like fold and a long chain fatty acid in a deep cleft (shaded red).This crystal structure shows a conserved hypothetical protein from M. tuberculosis. Only 12 other proteins share its sequence homology, and none has a known function. This structure indicates the protein may play a role in metabolic pathways. Credit: Integrated Center for Structure and Function InnovationCrystal structure of the beta2-adrenergic receptor protein. This is the first known structure of a human G protein-coupled receptor, a large family of proteins that control critical bodily functions and the action of about half of today’s pharmaceuticals. Credit: The Stevens Laboratory, The Scripps Research InstituteCrystal structure of a protein with unknown function from Xanthomonas campestris, a plant pathogen. Eight copies of the protein crystallized to form a ring. Holiday graphic created by Ken Schwinn and Sonia Espejon-Reynes, New York SGX Research Center for Structural Genomics.The crystal structure of the intracellular domain of ZntB, a transport protein that mediates the outflow of excess and potentially toxic metal ions. This protein is from the bacterium Vibrio parahaemolyticus, which can cause gastrointestinal illnesses in humans, and is found in other bacteria and plants. Credit: Midwest Center for Structural GenomicThis image represents the structure of TrpRS, a novel member of the tryptophanyl tRNA-synthetase family of enzymes. By helping to link the amino acid tryptophan to a tRNA molecule, TrpRS primes the amino acid for use in protein synthesis. A cluster of iron and sulfur atoms (orange and red spheres) was unexpectedly found in the anti-codon domain, a key part of the molecule, and appears to be critical for the function of the enzyme. TrpRS was discovered in Thermotoga maritima, a rod-shaped bacterium that flourishes in high temperatures. Credit: Joint Center for Structural Genomics
This page last updated August 6, 2008