Abstract
Rubisco enzymes play central roles in carbon fixation, with potential importance in biotechnology, but have eluded a full description of their multistep assembly and function. A new article describes the fascinating discovery that some archaeal Rubiscos contain a built-in assembly domain inserted into an otherwise canonical Rubisco fold, providing a tremendous expansion of our understanding of the diversity of naturally occurring Rubiscos.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 6851-6852 |
| Number of pages | 2 |
| Journal | Journal of Biological Chemistry |
| Volume | 292 |
| Issue number | 16 |
| DOIs | |
| State | Published - Apr 21 2017 |
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ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology
Cite this
A peptide adhesive molded by magnesium glues Rubisco's subunits together. / Wachter, Rebekka.
In: Journal of Biological Chemistry, Vol. 292, No. 16, 21.04.2017, p. 6851-6852.Research output: Contribution to journal › Review article
}
TY - JOUR
T1 - A peptide adhesive molded by magnesium glues Rubisco's subunits together
AU - Wachter, Rebekka
PY - 2017/4/21
Y1 - 2017/4/21
N2 - Rubisco enzymes play central roles in carbon fixation, with potential importance in biotechnology, but have eluded a full description of their multistep assembly and function. A new article describes the fascinating discovery that some archaeal Rubiscos contain a built-in assembly domain inserted into an otherwise canonical Rubisco fold, providing a tremendous expansion of our understanding of the diversity of naturally occurring Rubiscos.
AB - Rubisco enzymes play central roles in carbon fixation, with potential importance in biotechnology, but have eluded a full description of their multistep assembly and function. A new article describes the fascinating discovery that some archaeal Rubiscos contain a built-in assembly domain inserted into an otherwise canonical Rubisco fold, providing a tremendous expansion of our understanding of the diversity of naturally occurring Rubiscos.
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UR - http://www.scopus.com/inward/citedby.url?scp=85018538295&partnerID=8YFLogxK
U2 - 10.1074/jbc.H116.767145
DO - 10.1074/jbc.H116.767145
M3 - Review article
C2 - 28432177
AN - SCOPUS:85018538295
VL - 292
SP - 6851
EP - 6852
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 16
ER -