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Structure and Function of a Bacterial Microcompartment Shell Protein Engineered to Bind a [4Fe-4S] Cluster

Overview of attention for article published in Journal of the American Chemical Society, January 2016
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About this Attention Score

  • In the top 5% of all research outputs scored by Altmetric
  • High Attention Score compared to outputs of the same age (98th percentile)
  • High Attention Score compared to outputs of the same age and source (98th percentile)

Mentioned by

news
11 news outlets
blogs
3 blogs
twitter
6 X users
patent
3 patents
wikipedia
2 Wikipedia pages

Readers on

mendeley
95 Mendeley
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Article details
Title
Structure and Function of a Bacterial Microcompartment Shell Protein Engineered to Bind a [4Fe-4S] Cluster
Published in
Journal of the American Chemical Society, January 2016
DOI 10.1021/jacs.5b11734
Pubmed ID
Authors
Abstract

Bacterial microcompartments (BMCs) are self-assembling organelles composed of a selectively permeable protein shell and encapsulated enzymes. They are considered promising templates for the engineering of designed bio-nanoreactors for biotechnology. In particular, encapsulation of oxidoreductive reactions requiring electron transfer between the lumen of the BMC and the cytosol relies on the ability to conduct electrons across the shell. We determined the crystal structure of a component protein of a synthetic BMC shell, which informed the rational design of a [4Fe-4S] cluster-binding site in its pore. We also solved the structure of the [4Fe-4S] cluster-bound, engineered protein to 1.8 Å resolution, providing the first structure of a BMC shell protein containing a metal center. The [4Fe-4S] cluster was characterized by optical and EPR spectroscopies; it has a reduction potential of -370 mV vs. the Standard Hydrogen Electrode (SHE) and is stable through redox cycling. This remarkable stability may be attributable to the hydrogen bonding network provided by the main chain of the protein scaffold. The properties of the [4Fe-4S] cluster resemble those in low-potential bacterial ferredoxins, while its ligation to three cysteine residues is reminiscent of enzymes such as aconitase and radical S-adenosymethionine (SAM) enzymes. This engineered shell protein provides the foundation for conferring electron transfer functionality to BMC shells.

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X Demographics

X Demographics

The data shown below were collected from the profiles of 6 X users who shared this research output. Click here to find out more about how the information was compiled.
Mendeley demographics

Mendeley demographics

The data shown below were compiled from readership statistics for 95 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Geographical breakdown
Country Count As %
United States 3 3%
Japan 1 1%
Unknown 91 96%

Demographic breakdown

Readers by professional status
Readers by professional status Count As %
Student > Ph. D. Student 20 21%
Researcher 18 19%
Student > Bachelor 12 13%
Student > Master 8 8%
Student > Doctoral Student 7 7%
Other 12 13%
Unknown 18 19%
Readers by discipline
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 33 35%
Chemistry 21 22%
Agricultural and Biological Sciences 15 16%
Chemical Engineering 1 1%
Psychology 1 1%
Other 4 4%
Unknown 20 21%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 101. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 08 November 2022.
All research outputs
#502,443
of 31,301,153 outputs
Outputs from Journal of the American Chemical Society
#314
of 81,359 outputs
Outputs of similar age
#7,034
of 424,155 outputs
Outputs of similar age from Journal of the American Chemical Society
#7
of 476 outputs
Altmetric has tracked 31,301,153 research outputs across all sources so far. Compared to these this one has done particularly well and is in the 98th percentile: it's in the top 5% of all research outputs ever tracked by Altmetric.
So far Altmetric has tracked 81,359 research outputs from this source. They typically receive a little more attention than average, with a mean Attention Score of 7.4. This one has done particularly well, scoring higher than 99% of its peers.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 424,155 tracked outputs that were published within six weeks on either side of this one in any source. This one has done particularly well, scoring higher than 98% of its contemporaries.
We're also able to compare this research output to 476 others from the same source and published within six weeks on either side of this one. This one has done particularly well, scoring higher than 98% of its contemporaries.