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Three-dimensional Structure of Thermolysin

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TLDR
The electron density map of thermolysin indicates how the polypeptide chain is displaced throughout the overall shape of the molecule.
Abstract
The electron density map of thermolysin indicates how the polypeptide chain is displaced throughout the overall shape of the molecule.

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Recent Advances in Zinc Enzymology

TL;DR: Zinc enzymology is, compared to some other current areas of metallobiochemistry, a maturing field, but in addition to further developments of structure-function relationships it has also provided a number of surprising new results and ideas in the last few years.
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Zinc proteins: enzymes, storage proteins, transcription factors, and replication proteins.

TL;DR: The rapid increase in the number and nature of the proteins in which zinc functions is not unexpected since zinc is the second most abundant trace metal found in eukaryotic organisms, second only to iron.
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Function and mechanism of zinc metalloenzymes.

TL;DR: These studies demonstrate that the chemical nature of the direct ligands and the structure of the surrounding hydrogen bond network are crucial for both the activity of carbonic anhydrase and the metal ion affinity of the zinc-binding site.
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Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the 'metzincins'

TL;DR: X‐ray crystal structures of two zinc endopeptidases, astacin from crayfish and adamalysin II from snake venom, reveal a strong overall topological equivalence and virtually identical extended HEXXHXXGXXH zinc‐binding segments, but in addition a methionine‐containing turn of similar conformation (the ‘Met‐turn’), which forms a hydrophobic basis for the zinc ion and the three liganding histidine residues.
References
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Journal ArticleDOI

The structure of proteins; two hydrogen-bonded helical configurations of the polypeptide chain.

TL;DR: This work has used information about interatomic distances, bond angles, and other configurational parameters to construct two reasonable hydrogen-bonded helical configurations for the polypeptide chain; it is likely that these configurations constitute an important part of the structure of both fibrous and globular proteins, as well as of syntheticpolypeptides.
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Structure of hen egg-white lysozyme. A three-dimensional Fourier synthesis at 2 Angstrom resolution.

TL;DR: Structure of Hen Egg-White Lysozyme: A Three-dimensional Fourier Synthesis at 2 A Resolution as mentioned in this paper, 3D Fourier synthesis at 2 a resolution.
Journal ArticleDOI

Structure of subtilisin BPN' at 2.5 angström resolution.

TL;DR: In this paper, a single polypeptide chain is folded into three parts, with the active site at their conjunction, and the side chain of His 64 is in a position consistent with the formation of a hydrogen bond between it and the OH group of Ser 221.
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