A leucine-rich repeat variant with a novel repetitive protein structural motif

@article{Peters1996ALR,
  title={A leucine-rich repeat variant with a novel repetitive protein structural motif},
  author={John W. Peters and Michael H. B. Stowell and Douglas C. Rees},
  journal={Nature Structural Biology},
  year={1996},
  volume={3},
  pages={991-994}
}
The structure of the leucine-rich repeat variant protein reveals a novel fold consisting of alternating α- and 3_(10)-helices arranged in a right-handed superhelix that follows an N-terminal 4Fe:4S cluster-containing domain. 
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53 Citations
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Citation Type

Leucines on a roll
  • B. Kobe
  • Physics, Biology
    Nature Structural Biology
  • 1996
TLDR
The structure of the leucine-rich repeat variant protein represents an unexpected addition to the list of such proteins, with the repetitive unit consisting of antiparallel alpha- and 3(10)-helices.
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The leucine-rich repeat structure
TLDR
An update of the current understanding of leucine-rich repeat structure at the primary, secondary, tertiary and quaternary levels is presented and specific examples from recently determined three-dimensional structures are discussed.
When protein folding is simplified to protein coiling: the continuum of solenoid protein structures.
Turn up the HEAT.
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Crystal structure of transcription factor MalT domain III: a novel helix repeat fold implicated in regulated oligomerization.
The architecture of parallel β-helices and related folds
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References

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TLDR
This work has determined the crystal structure of the porcine inhibitor, which is the first three-dimensional structure of a protein containing leucine-rich repeats and represents a new class of α/β protein fold.
Short alanine-based peptides may form 310-helices and not α-helices in aqueous solution
TLDR
The experiments suggest that the more likely peptide geometry is a 310-helix, and single and doubly spin-labelled analogues of alanine-based peptides in which the nitroxide spin label forms an unbranched side chain extending from the sulphur atom of a cysteine residue are designed.
Identification of a nitrogenase protein-protein interaction site defined by residues 59 through 67 within the Azotobacter vinelandii Fe protein.
PROMOTIF—A program to identify and analyze structural motifs in proteins
TLDR
A suite of programs, PROMOTIF, that analyzes a protein coordinate file and provides details about the structural motifs in the protein, and can also be used to compare motifS in a group of related structures, such as an ensemble of NMR structures.
Helix geometry in proteins.
Crystallographic structure of the nitrogenase iron protein from Azotobacter vinelandii.
TLDR
The crystal structure of the nitrogenase Fe-protein from Azotobacter vinelandii has been determined and it appears that interactions between the nucleotide and cluster sites must be indirectly coupled by allosteric changes occurring at the subunit interface.
A program to produce both detailed and schematic plots of protein structures
The MOLSCRIPT program produces plots of protein structures using several different kinds of representations. Schematic drawings, simple wire models, ball-and-stick models, CPK models and text labels…
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