High-Resolution Structure of the Diphtheria Toxin Repressor Complexed with Cobalt and Manganese Reveals an SH3-like Third Domain and Suggests a Possible Role of Phosphate as Co-corepressor†,‡

Biochemistry ◽  
1996 ◽  
Vol 35 (38) ◽  
pp. 12292-12302 ◽  
Author(s):  
Xiayang Qiu ◽  
Ehmke Pohl ◽  
Randall K. Holmes ◽  
Wim G. J. Hol
Keyword(s):  
High Resolution ◽  
Diphtheria Toxin ◽  
Diphtheria Toxin Repressor ◽  
High Resolution Structure ◽  
Resolution Structure

What we have learned from ribosome structures

2008 ◽  
Vol 36 (4) ◽  
pp. 567-574 ◽  
Author(s):  
V. Ramakrishnan
Keyword(s):  
High Resolution ◽  
Ribosomal Subunit ◽  
Ribosomal Subunits ◽  
30S Subunit ◽  
High Resolution Structure ◽  
70S Ribosome ◽  
Year 2000 ◽  
Resolution Structure

The determination of the high-resolution structures of ribosomal subunits in the year 2000 and of the entire ribosome a few years later are revolutionizing our understanding of the role of the ribosome in translation. In the present article, I summarize the main contributions from our laboratory to this worldwide effort. These include the determination of the structure of the 30S ribosomal subunit and its complexes with antibiotics, the role of the 30S subunit in decoding, and the high-resolution structure of the entire 70S ribosome complexed with mRNA and tRNA.

scholarly journals Structural Basis for Cytoplasmic Dynein-1 Regulation by Lis1

2021 ◽  
Author(s):  
John P Gillies ◽  
Janice M Reimer ◽  
Eva P Karasmanis ◽  
Indrajit Lahiri ◽  
Zaw Min Htet ◽  
...  
Keyword(s):  
High Resolution ◽  
Cytoplasmic Dynein ◽  
Motor Domain ◽  
Structural Basis ◽  
Neurodevelopmental Disease ◽  
Microtubule Motor ◽  
High Resolution Structure ◽  
Resolution Structure

The lissencephaly 1 gene, LIS1, is mutated in patients with the neurodevelopmental disease lissencephaly. The Lis1 protein is conserved from fungi to mammals and is a key regulator of cytoplasmic dynein-1, the major minus-end-directed microtubule motor in many eukaryotes. Lis1 is the only dynein regulator that binds directly to dynein's motor domain, and by doing so alters dynein's mechanochemistry. Lis1 is required for the formation of fully active dynein complexes, which also contain essential cofactors: dynactin and an activating adaptor. Here, we report the first high-resolution structure of the yeast dynein-Lis1 complex. Our 3.1Å structure reveals, in molecular detail, the major contacts between dynein and Lis1 and between Lis1's β-propellers. Structure-guided mutations in Lis1 and dynein show that these contacts are required for Lis1's ability to form fully active human dynein complexes and to regulate yeast dynein's mechanochemistry and in vivo function. We present a model for the conserved role of Lis1 in regulating dynein from yeast to humans.

scholarly journals High-resolution structure of podovirus tail adaptor suggests repositioning of an octad motif that mediates the sequential tail assembly

2017 ◽  
Vol 115 (2) ◽  
pp. 313-318 ◽  
Author(s):  
Lingfei Liang ◽  
Haiyan Zhao ◽  
Bowen An ◽  
Liang Tang
Keyword(s):  
High Resolution ◽  
Adaptor Protein ◽  
Underlying Mechanism ◽  
Life Cycles ◽  
Sequence Motif ◽  
Ring Model ◽  
High Resolution Structure ◽  
Two Sides ◽  
Resolution Structure

The sophisticated tail structures of DNA bacteriophages play essential roles in life cycles. Podoviruses P22 and Sf6 have short tails consisting of multiple proteins, among which is a tail adaptor protein that connects the portal protein to the other tail proteins. Assembly of the tail has been shown to occur in a sequential manner to ensure proper molecular interactions, but the underlying mechanism remains to be understood. Here, we report the high-resolution structure of the tail adaptor protein gp7 from phage Sf6. The structure exhibits distinct distribution of opposite charges on two sides of the molecule. A gp7 dodecameric ring model shows an entirely negatively charged surface, suggesting that the assembly of the dodecamer occurs through head-to-tail interactions of the bipolar monomers. The N-terminal helix-loop structure undergoes rearrangement compared with that of the P22 homolog complexed with the portal, which is achieved by repositioning of two consecutive repeats of a conserved octad sequence motif. We propose that the conformation of the N-terminal helix-loop observed in the Sf6-gp7 and P22 portal:gp4 complex represents the pre- and postassembly state, respectively. Such motif repositioning may serve as a conformational switch that creates the docking site for the tail nozzle only after the assembly of adaptor protein to the portal. In addition, the C-terminal portion of gp7 shows conformational flexibility, indicating an induced fit on binding to the portal. These results provide insight into the mechanistic role of the adaptor protein in mediating the sequential assembly of the phage tail.

scholarly journals High-resolution structure determination by continuous-rotation data collection in MicroED

2014 ◽  
Vol 11 (9) ◽  
pp. 927-930 ◽  
Author(s):  
Brent L Nannenga ◽  
Dan Shi ◽  
Andrew G W Leslie ◽  
Tamir Gonen
Keyword(s):  
High Resolution ◽  
Data Collection ◽  
Structure Determination ◽  
Continuous Rotation ◽  
High Resolution Structure ◽  
Resolution Structure

scholarly journals Tricks of the trade used to accelerate high-resolution structure determination of membrane proteins

FEBS Letters ◽  
2010 ◽  
Vol 584 (12) ◽  
pp. 2539-2547 ◽  
Author(s):  
Yo Sonoda ◽  
Alex Cameron ◽  
Simon Newstead ◽  
Hiroshi Omote ◽  
Yoshinori Moriyama ◽  
...  
Keyword(s):  
High Resolution ◽  
Membrane Proteins ◽  
Structure Determination ◽  
High Resolution Structure ◽  
Resolution Structure
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