Andreas Kuglstatter
Max Planck Society
12 Papers
198 Citations
Andreas Kuglstatter is an academic researcher from Max Planck Society. The author has contributed to research in topics: Rhodobacter sphaeroides & Photosynthetic reaction centre. The author has an hindex of 8, co-authored 12 publications. Previous affiliations of Andreas Kuglstatter include Laboratory of Molecular Biology.
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Papers
Induced structural changes of 7SL RNA during the assembly of human signal recognition particle
TL;DR: The crystal structure of the ternary complex suggests why SRP19 is necessary for the stable binding of SRP54 to the S domain RNA.
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Crystal Structure of SRP19 in Complex with the S Domain of SRP RNA and Its Implication for the Assembly of the Signal Recognition Particle
TL;DR: The crystal structure of Methanococcus jannaschii SRP19 bound to the S domain of human 7SL RNA at 2.9 A resolution is determined, which indicates that the particle clamps the tetraloops of two branched helices and allows them to interact side by side.
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Structure and Assembly of the Spliceosomal snRNPs
Kiyoshi Nagai,Yutaka Muto,D. A. Pomeranz Krummel,C. Kambach,T. Ignjatovic,S. Walke,Andreas Kuglstatter +6 more
TL;DR: The X-ray crystal structure of some snRNP proteins as part of either protein- protein complexes or RNA-protein complexes has provided an important insight into the overall architecture of the U1 and U2 snRNPs and the mechanisms of RNA- protein and protein-protein recognition.
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X-ray Structure Analyses of Photosynthetic Reaction Center Variants from Rhodobacter sphaeroides: Structural Changes Induced by Point Mutations at Position L209 Modulate Electron and Proton Transfer†
TL;DR: The structure of the Pro L209 --> Tyr variant, Q(B) is shifted by approximately 4 A and is now located at a position similar to that reported for the wild-type reaction center after illumination, and the binding site of Q( B) remains unchanged compared to theWild-type structure.
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Charge separation induces conformational changes in the photosynthetic reaction centre of purple bacteria
TL;DR: X-ray structures of the wild-type reaction centre from Rhodobacter sphaeroides have been determined and the structure of the mutant RC L 209 PY that keeps the Q(B) molecule in the proximal position even in the charge-neutral state is compared.
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