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.

2.50
Hdl Handle:
http://hdl.handle.net/10033/23156
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.
Authors:
Peters, Katrin; Dudkina, Natalya V; Jänsch, Lothar ( 0000-0002-5655-1181 ) ; Braun, Hans-Peter; Boekema, Egbert J
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.
Affiliation:
Institute for Plant Genetics, Faculty of Natural Sciences, Leibniz Universität Hannover, Herrenhäuser Str. 2, D-30419 Hannover, Germany.
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
Journal:
Biochimica et biophysica acta
Issue Date:
Jan-2008
URI:
http://hdl.handle.net/10033/23156
DOI:
10.1016/j.bbabio.2007.10.012
PubMed ID:
18047828
Type:
Article
Language:
en
ISSN:
0006-3002
Appears in Collections:
publications of the research group cellular proteom research (CPRO)

Full metadata record

DC FieldValue Language
dc.contributor.authorPeters, Katrinen
dc.contributor.authorDudkina, Natalya Ven
dc.contributor.authorJänsch, Lotharen
dc.contributor.authorBraun, Hans-Peteren
dc.contributor.authorBoekema, Egbert Jen
dc.date.accessioned2008-04-14T09:41:58Zen
dc.date.available2008-04-14T09:41:58Zen
dc.date.issued2008-01en
dc.identifier.citationA 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. Actaen
dc.identifier.issn0006-3002en
dc.identifier.pmid18047828en
dc.identifier.doi10.1016/j.bbabio.2007.10.012en
dc.identifier.urihttp://hdl.handle.net/10033/23156en
dc.description.abstractThe 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.en
dc.language.isoenen
dc.subject.meshAmino Acid Sequenceen
dc.subject.meshArabidopsisen
dc.subject.meshCarbonic Anhydrasesen
dc.subject.meshElectron Transport Complex Ien
dc.subject.meshElectron Transport Complex IIIen
dc.subject.meshMicroscopy, Electronen
dc.subject.meshMolecular Sequence Dataen
dc.subject.meshProtein Structure, Tertiaryen
dc.subject.meshZea maysen
dc.titleA 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.typeArticleen
dc.contributor.departmentInstitute for Plant Genetics, Faculty of Natural Sciences, Leibniz Universität Hannover, Herrenhäuser Str. 2, D-30419 Hannover, Germany.en
dc.identifier.journalBiochimica et biophysica actaen

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