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The crystal structure of polygalacturonase-inhibiting protein (PGIP), a leucine-rich repeat protein involved in plant defense
TLDR
The crystal structure at 1.7-Å resolution of a PGIP is reported, characterized by the presence of two β-sheets instead of the single one originally predicted by modeling studies, and reveals a negatively charged surface on the LRR concave face, likely involved in binding polygalacturonases. Expand
Structural requirements of endopolygalacturonase for the interaction with PGIP (polygalacturonase-inhibiting protein)
TLDR
The structure of FmPG was useful to study the mode of interaction of the enzyme with PGIP-2 from Phaseolus vulgaris, and it is suggested that variations are important structural requirements of plant PGs to prevent PGIP binding. Expand
The structure of ActVA‐Orf6, a novel type of monooxygenase involved in actinorhodin biosynthesis
TLDR
This is the first crystal structure of an enzyme involved in the tailoring of a type II aromatic polyketide and illustrates some of the enzyme–substrate recognition features that may apply to a range of other enzymes involved in modifying apolyketide core structure. Expand
The crystal structure of saporin SO6 from Saponaria officinalis and its interaction with the ribosome
TLDR
Structural comparison between saporin and other ribosome inactivating proteins reveals that this region is conserved and represents a peculiar motif involved in ribosomes recognition, suggesting an easier access to the substrate. Expand
Insights into DNA replication: the crystal structure of DNA polymerase B1 from the archaeon Sulfolobus solfataricus.
TLDR
The structural basis of specific lesion recognition, the initial step in DNA repair, is explored, describing how the N-terminal subdomain pocket of archaeal DNA polymerases could allow specific recognition of deaminated bases such as uracil and hypoxanthine in addition to the typical DNA bases. Expand
Investigating the Structural Plasticity of a Cytochrome P450
TLDR
Analysis of three-dimensional structures of a monomeric cytochrome P450 from Saccharopolyspora erythraea and the binding kinetics to its physiological ligand demonstrated that EryK binds erystromycin D via a mechanism involving at least two steps, confirmed that this complex scenario arises from a pre-existing equilibrium between the open and closed subpopulations of Eryk. Expand
Glyphosate Resistance by Engineering the Flavoenzyme Glycine Oxidase*
TLDR
It is proposed that the enzymatic oxidation of glyphosate could be an effective alternative to this important biotechnological process and a rational design approach is used to generate a glycine oxidase variant more active on glyphosate than on the physiological substrate glycine. Expand
Structural dynamics of ligand diffusion in the protein matrix: A study on a new myoglobin mutant Y(B10) Q(E7) R(E10).
TLDR
The hypothesis may rationalize the O2 binding properties of Mb-YQR and more generally to propose a mechanism of control of ligand binding and dissociation in hemeproteins based on the dynamics of side chains that may allow access to and direct temporary sequestration of the dissociated ligand in a docking site within the protein. Expand
Pattern of cavities in globins: The case of human hemoglobin
TLDR
The pattern of internal cavities accessibility and affinity for xenon suggests a different role for the dynamics of ligand migration in the two types of hemoglobin chains as compared to myoglobin. Expand
Crystal structure of Trematomus newnesi haemoglobin re-opens the root effect question.
TLDR
The structure of Trematomus newnesi Hb 1 is similar to that of Root effect fish Hbs from Spot and T. bernacchii, suggesting that the differences in the pH dependence cannot be related to the modulation of the R-state. Expand
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