A structural investigation of complex I and I+III2 supercomplex from Zea mays at 11-13 A resolution: assignment of the carbonic anhydrase domain and evidence for structural heterogeneity within complex I.
dc.contributor.author | Peters, Katrin | |
dc.contributor.author | Dudkina, Natalya V | |
dc.contributor.author | Jänsch, Lothar | |
dc.contributor.author | Braun, Hans-Peter | |
dc.contributor.author | Boekema, Egbert J | |
dc.date.accessioned | 2008-04-14T09:41:58Z | en |
dc.date.available | 2008-04-14T09:41:58Z | en |
dc.date.issued | 2008-01 | en |
dc.identifier.citation | A structural investigation of complex I and I+III2 supercomplex from Zea mays at 11-13 A resolution: assignment of the carbonic anhydrase domain and evidence for structural heterogeneity within complex I. 2008, 1777 (1):84-93 Biochim. Biophys. Acta | en |
dc.identifier.issn | 0006-3002 | en |
dc.identifier.pmid | 18047828 | en |
dc.identifier.doi | 10.1016/j.bbabio.2007.10.012 | en |
dc.identifier.uri | http://hdl.handle.net/10033/23156 | en |
dc.description.abstract | The projection structures of complex I and the I+III2 supercomplex from the C4 plant Zea mays were determined by electron microscopy and single particle image analysis to a resolution of up to 11 A. Maize complex I has a typical L-shape. Additionally, it has a large hydrophilic extra-domain attached to the centre of the membrane arm on its matrix-exposed side, which previously was described for Arabidopsis and which was reported to include carbonic anhydrase subunits. A comparison with the X-ray structure of homotrimeric gamma-carbonic anhydrase from the archaebacterium Methanosarcina thermophila indicates that this domain is also composed of a trimer. Mass spectrometry analyses allowed to identify two different carbonic anhydrase isoforms, suggesting that the gamma-carbonic anhydrase domain of maize complex I most likely is a heterotrimer. Statistical analysis indicates that the maize complex I structure is heterogeneous: a less-abundant "type II" particle has a 15 A shorter membrane arm and an additional small protrusion on the intermembrane-side of the membrane arm if compared to the more abundant "type I" particle. The I+III2 supercomplex was found to be a rigid structure which did not break down into subcomplexes at the interface between the hydrophilic and the hydrophobic arms of complex I. The complex I moiety of the supercomplex appears to be only of "type I". This would mean that the "type II" particles are not involved in the supercomplex formation and, hence, could have a different physiological role. | |
dc.language.iso | en | en |
dc.subject.mesh | Amino Acid Sequence | en |
dc.subject.mesh | Arabidopsis | en |
dc.subject.mesh | Carbonic Anhydrases | en |
dc.subject.mesh | Electron Transport Complex I | en |
dc.subject.mesh | Electron Transport Complex III | en |
dc.subject.mesh | Microscopy, Electron | en |
dc.subject.mesh | Molecular Sequence Data | en |
dc.subject.mesh | Protein Structure, Tertiary | en |
dc.subject.mesh | Zea mays | en |
dc.title | A structural investigation of complex I and I+III2 supercomplex from Zea mays at 11-13 A resolution: assignment of the carbonic anhydrase domain and evidence for structural heterogeneity within complex I. | en |
dc.type | Article | en |
dc.contributor.department | Institute for Plant Genetics, Faculty of Natural Sciences, Leibniz Universität Hannover, Herrenhäuser Str. 2, D-30419 Hannover, Germany. | en |
dc.identifier.journal | Biochimica et biophysica acta | en |
refterms.dateFOA | 2018-06-12T22:44:13Z | |
html.description.abstract | The projection structures of complex I and the I+III2 supercomplex from the C4 plant Zea mays were determined by electron microscopy and single particle image analysis to a resolution of up to 11 A. Maize complex I has a typical L-shape. Additionally, it has a large hydrophilic extra-domain attached to the centre of the membrane arm on its matrix-exposed side, which previously was described for Arabidopsis and which was reported to include carbonic anhydrase subunits. A comparison with the X-ray structure of homotrimeric gamma-carbonic anhydrase from the archaebacterium Methanosarcina thermophila indicates that this domain is also composed of a trimer. Mass spectrometry analyses allowed to identify two different carbonic anhydrase isoforms, suggesting that the gamma-carbonic anhydrase domain of maize complex I most likely is a heterotrimer. Statistical analysis indicates that the maize complex I structure is heterogeneous: a less-abundant "type II" particle has a 15 A shorter membrane arm and an additional small protrusion on the intermembrane-side of the membrane arm if compared to the more abundant "type I" particle. The I+III2 supercomplex was found to be a rigid structure which did not break down into subcomplexes at the interface between the hydrophilic and the hydrophobic arms of complex I. The complex I moiety of the supercomplex appears to be only of "type I". This would mean that the "type II" particles are not involved in the supercomplex formation and, hence, could have a different physiological role. |