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The binding of Maize DHN1 to Lipid Vesicles. Gain of Structure and Lipid Specificity1
It is shown that maize (Zea mays) DHN DHN1 can bind to lipid vesicles that contain acidic phospholipids, and that the association ofDHN1 with vesicle results in an apparent increase of α-helicity of the protein.
Structure and mechanism of ABC transporters
- S. Wilkens
- BiologyF1000prime reports
- 3 February 2015
Recent progress with the X-ray crystal structure determination of a variety of bacterial and eukaryotic ABC transporters has helped to advance the understanding of the ATP hydrolysis-driven transport mechanism but has also illustrated the large structural and functional diversity within the family.
The K-Segment of Maize DHN1 Mediates Binding to Anionic Phospholipid Vesicles and Concomitant Structural Changes1[W][OA]
Lipop vesicle-binding assays revealed that the K-segment is required for binding to anionic phospholipid vesicles, and adoption of α-helicity of the K, a structural element known to interact with membranes and proteins, accounts for most of the conformational change of DHNs.
An Endoplasmic Reticulum (ER) Membrane Complex Composed of SPFH1 and SPFH2 Mediates the ER-associated Degradation of Inositol 1,4,5-Trisphosphate Receptors*
- Margaret M. P. Pearce, D. Wormer, S. Wilkens, R. Wojcikiewicz
- BiologyJournal of Biological Chemistry
- 17 April 2009
This work reports that the ER membrane protein SPFH1 and its homolog SPFH2 form a heteromeric ∼2 MDa complex that binds to IP3R tetramers immediately after their activation and is required for their processing.
Structure of dimeric mitochondrial ATP synthase: novel F0 bridging features and the structural basis of mitochondrial cristae biogenesis.
- F. Minauro-Sanmiguel, S. Wilkens, J. J. Garcia
- Biology, ChemistryProceedings of the National Academy of Sciences…
- 30 August 2005
The structure of the dimeric F1F0-ATP synthase complex isolated from bovine heart mitochondria by transmission electron microscopy has an overall conic appearance that is consistent with the proposed role of theDimeric enzyme in mitochondrial cristae biogenesis.
Crystal structure of the yeast vacuolar ATPase heterotrimeric EGC(head) peripheral stalk complex.
Structure of the Yeast Vacuolar ATPase*
The resulting atomic model of the yeast V-ATPase serves as a framework to help understand the role the peripheral stalk subunits are playing in the regulation of the ATP hydrolysis driven proton pumping activity of the vacuolar ATPase.
Structure of the Vacuolar ATPase by Electron Microscopy*
The structure of the vacuolar ATPase from bovine brain clathrin-coated vesicles has been determined by electron microscopy of negatively stained, detergent-solubilized enzyme molecules, confirming their common origin.
Mgm101 Is a Rad52-related Protein Required for Mitochondrial DNA Recombination*
- MacMillan Mbantenkhu, Xiaowen Wang, Xin Jie Chen
- BiologyThe Journal of Biological Chemistry
- 25 October 2011
It is shown that the yeast mitochondrial nucleoid protein, Mgm101, is related to the Rad52-type recombination proteins that are widespread in organisms from bacteriophage to humans.