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Robert Huber

Researcher at Technische Universität München

Publications -  742
Citations -  76282

Robert Huber is an academic researcher from Technische Universität München. The author has contributed to research in topics: Active site & Protein structure. The author has an hindex of 139, co-authored 671 publications receiving 73557 citations. Previous affiliations of Robert Huber include Munich University of Applied Sciences & Russian Academy of Sciences.

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Journal ArticleDOI

Structural basis for Ca2+-independence and activation by homodimerization of tomato subtilase 3

TL;DR: This work reports the first structure of a plant subtilase, SBT3 from tomato, in the active apo form and complexed with a chloromethylketone (cmk) inhibitor and presents the first structural evidence for an explicit function of PA domains in proteases revealing a vital role in the homo-dimerization ofSBT3 and in enzyme activation.
Book ChapterDOI

Structure quality and target parameters

TL;DR: In this paper, a set of bond and angle target parameters derived from small-molecule structures in the Cambridge Structural Database and their application to the refinement of protein structure models are discussed.
Journal ArticleDOI

A dissimilatory sirohaem-sulfite-reductase-type protein from the hyperthermophilic archaeon Pyrobaculum islandicum.

TL;DR: Phylogenetic analyses indicate a common protogenotic origin of the P. islandicum protein and the dissimilatory sulfite reductases from sulfate-reducing and sulfide-oxidizing prokaryotes most probably evolved into three independent lineages prior to divergence of archaea and bacteria.
Journal ArticleDOI

The substrate translocation channel of the proteasome.

TL;DR: These results identify a specific mechanism for allosteric regulation of the CP by the RP, and show that open-channel mutations in CP subunits suppress the closed-channel phenotype of an rpt2 mutant.
Journal ArticleDOI

Crystal structure of MunI restriction endonuclease in complex with cognate DNA at 1.7 Å resolution

TL;DR: The MunI restriction enzyme recognizes the palindromic hexanucleotide sequence C/AATTG and the crystal structure of its active site mutant D83A bound to cognate DNA has been determined at 1.7 Å resolution.