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The 8 most recent public experiments

The Zn inactive class of glyoxalase I (Glo1) enzymes are metalloenzymes that are typically homodimeric with two metal-dependent active sites. While the two active sites share identical amino acid composition, this class of enzyme is optimally active with only one metal per homodimer. We have determined the X-ray crystal structure of GloA2, one of the Zn inactive Glo1 enzymes from Pseudomonas aeruginosa. The presented structures exhibit an unprecedented metal-binding arrangement consistent with half-of-sites activity: one active site contains a single activating Ni2+ ion while the other contains two inactivating Zn2+ ions. Students from UWA CHEM3007 Undergraduate Unit helped with some of the data collection.

The Zn inactive class of glyoxalase I (Glo1) enzymes are metalloenzymes that are typically homodimeric with two metal-dependent active sites. While the two active sites share identical amino acid composition, this class of enzyme is optimally active with only one metal per homodimer. We have determined the X-ray crystal structure of GloA2, one of the Zn inactive Glo1 enzymes from Pseudomonas aeruginosa. The presented structures exhibit an unprecedented metal-binding arrangement consistent with half-of-sites activity: one active site contains a single activating Ni2+ ion while the other contains two inactivating Zn2+ ions. Students from UWA CHEM3007 Undergraduate Unit helped with some of the data collection.

The Zn inactive class of glyoxalase I (Glo1) enzymes are metalloenzymes that are typically homodimeric with two metal-dependent active sites. While the two active sites share identical amino acid composition, this class of enzyme is optimally active with only one metal per homodimer. We have determined the X-ray crystal structure of GloA2, one of the Zn inactive Glo1 enzymes from Pseudomonas aeruginosa. The presented structures exhibit an unprecedented metal-binding arrangement consistent with half-of-sites activity: one active site contains a single activating Ni2+ ion while the other contains two inactivating Zn2+ ions. Students from UWA CHEM3007 Undergraduate Unit helped with some of the data collection.

The Zn inactive class of glyoxalase I (Glo1) enzymes are metalloenzymes that are typically homodimeric with two metal-dependent active sites. While the two active sites share identical amino acid composition, this class of enzyme is optimally active with only one metal per homodimer. We have determined the X-ray crystal structure of GloA2, one of the Zn inactive Glo1 enzymes from Pseudomonas aeruginosa. The presented structures exhibit an unprecedented metal-binding arrangement consistent with half-of-sites activity: one active site contains a single activating Ni2+ ion while the other contains two inactivating Zn2+ ions. Students from UWA CHEM3007 Undergraduate Unit helped with some of the data collection.

Defining the interaction of perforin with calcium and the phospholipid membrane Daouda A.K. Traore, James C Whisstock Download data as .tar

Following its secretion from cytotoxic lymphocytes into the immune synapse, perforin binds to target cell membranes through its Ca2 + -dependent C2 domain. Membrane-bound perforin then forms pores that allow passage of pro-apoptopic granzymes into the target cell. In the present study, structural and biochemical studiesrevealthatCa2+ bindingtriggersaconformationalchange in the C2 domain that permits four key hydrophobic residues to interact with the plasma membrane. However, in contrast with previous suggestions, these movements and membrane binding do not trigger irreversible conformational changes in the pore-forming MACPF (membrane attack complex/perforin- like) domain, indicating that subsequent monomer–monomer interactions at the membrane surface are required for perforin pore formation. Publication: Biochem J.

This is a test experiment.

Rotary ATPases couple ATP hydrolysis/synthesis with proton translocation across biological membranes and so are central components of the biological energy conversion machinery. Their peripheral stalks are essential components that counteract torque generated by rotation of the central stalk during ATP synthesis or hydrolysis. These datasets are derivatives of the peripheral stalk from T.thermophilus A-ATPase. Native crystals were soaked in Lutetium(III) acetate (2K7c_3_###.img) and Dysprosium(III) chloride (2K3#######.img). Resulting maps were used to create the pdb model 3V6I. The model was used to identify bending and twisting motions inherent within the structure that accommodate movements within the ATPase.

Structure-Informed Design of an Enzymatically Inactive Vaccine Component for Group A Streptococcus Anna Henningham, Daniel J. Ericsson, Karla Langer, Lachlan Casey, Blagojce Jovcevski, G. Singh Chhatwal, J. Andrew Aquilina, Michael R. Batzloff, Bostjan Kobe, Mark Walker Download data as .tar

Streptococcus pyogenes (group A Streptococcus [GAS]) causes ~700 million human infections/year, resulting in >500,000 deaths. There is no commercial GAS vaccine available. The GAS surface protein arginine deiminase (ADI) protects mice against a lethal challenge. ADI is an enzyme that converts arginine to citrulline and ammonia. Administration of a GAS vaccine preparation containing wild-type ADI, a protein with inherent enzymatic activity, may present a safety risk. In an approach intended to maximize the vaccine safety of GAS ADI, X-ray crystallography and structural immunogenic epitope mapping were used to inform vaccine design. This study aimed to knock out ADI enzyme activity without disrupting the three-dimensional structure or the recognition of immunogenic epitopes. We determined the crystal structure of ADI at 2.5 Å resolution and used it to select a number of amino acid residues for mutagenesis to alanine (D166, E220, H275, D277, and C401). Each mutant protein displayed abrogated activity, and three of the mutant proteins (those with the D166A, H275A, and D277A mutations) possessed a secondary structure and oligomerization state equivalent to those of the wild type, produced high-titer antisera, and avoided disruption of B-cell epitopes of ADI. In addition, antisera raised against the D166A and D277A mutant proteins bound to the GAS cell surface. The inactivated D166A and D277A mutant ADIs are ideal for inclusion in a GAS vaccine preparation. There is no human ortholog of ADI, and we confirm that despite limited structural similarity in the active-site region to human peptidyl ADI 4 (PAD4), ADI does not functionally mimic PAD4 and antiserum raised against GAS ADI does not recognize human PAD4.