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Crystal structure of the nickel–iron hydrogenase from Desulfovibrio gigas
TLDR
The X-ray structure of the heterodimeric Ni–Fe hydrogenase from Desulfovibrio gigas, the enzyme responsible for the metabolism of molecular hydrogen, has been solved at 2.85 Å resolution and suggests plausible electron and proton transfer pathways.
The Crystal Structure of the Globular Head of Complement Protein C1q Provides a Basis for Its Versatile Recognition Properties*
TLDR
The crystal structure of the C1q globular domain responsible for its recognition properties has now been solved and refined to 1.9 Å of resolution, revealing a compact, almost spherical heterotrimeric assembly held together mainly by non-polar interactions.
Crystal Structure of Human Butyrylcholinesterase and of Its Complexes with Substrate and Products*
TLDR
The crystal structures of several recombinant truncated human BChE complexes and conjugates are reported and a description for mechanistically relevant non-productive substrate and product binding is provided and is similar to a previously published theoretical model of this enzyme.
Structure of Dual Function Iron Regulatory Protein 1 Complexed with Ferritin IRE-RNA
TLDR
Extensive conformational changes related to binding the IRE or an iron-sulfur cluster explain the alternate functions of IRP1 as an mRNA regulator or enzyme.
Ni-Zn-[Fe4-S4] and Ni-Ni-[Fe4-S4] clusters in closed and open α subunits of acetyl-CoA synthase/carbon monoxide dehydrogenase
TLDR
It is postulate that only the A-clusters containing two Ni ions are catalytically active in the tetrameric α2β2 acetyl-coenzyme A synthase/carbon monoxide dehydrogenase from Moorella thermoacetica.
Crystal structures of the key anaerobic enzyme pyruvate:ferredoxin oxidoreductase, free and in complex with pyruvate
TLDR
The PFOR–pyruvate complex structure shows the noncovalent fixation of the substrate before the catalytic reaction, and the thiamin pyrophosphate cofactor and the three [4Fe–4S] clusters are suitably arranged to provide a plausible electron transfer pathway.
Structural insights into the innate immune recognition specificities of L‐ and H‐ficolins
TLDR
Human L‐ and H‐ficolins are soluble oligomeric defence proteins with lectin‐like activity, assembled from collagen fibers prolonged by fibrinogen‐like recognition domains, which define an unpredicted continuous recognition surface able to sense various acetylated and neutral carbohydrate markers in the context of extended polysaccharides such as 1,3‐β‐D‐glucan, as found on microbial or apoptotic surfaces.
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