Author pages are created from data sourced from our academic publisher partnerships and public sources.
Share This Author
Many paths to methyltransfer: a chronicle of convergence.
This work has shown how binding specificity is determined, how ubiquitin binding is regulated, and the function of UBDs in the context of full-length proteins is controlled by studying their mechanism of action.
Inositol Hexakisphosphate Is Bound in the ADAR2 Core and Required for RNA Editing
- M. MacBeth, H. Schubert, A. Vandemark, A. Lingam, C. Hill, B. Bass
- Biology, ChemistryScience
- 2 September 2005
It is shown that inositol hexakisphosphate (IP6) is required for activity in ADAR2, an RNA editing enzyme, and Amino acids that coordinate IP6 in the crystal structure are conserved in some adenosine deaminases that act on transfer RNA (tRNA) (ADATs), related enzymes that edit tRNA.
Structural Basis for ESCRT-III Protein Autoinhibition
It is shown that the N-terminal core domains of increased sodium tolerance-1 (IST1) and charged multivesicular body protein-3 (CHMP3) form equivalent four-helix bundles, revealing that IST1 is a previously unrecognized ESCRT-III family member.
Ubiquitin recognition by the human TSG101 protein.
Deficiency of glutaredoxin 5 reveals Fe–S clusters are required for vertebrate haem synthesis
It is shown that the hypochromic anaemia in shiraz (sir) zebrafish mutants is caused by deficiency of glutaredoxin 5 (grx5), a gene required in yeast for Fe–S cluster assembly, indicating that haemoglobin production in the differentiating red cell is regulated through Fe– S cluster assembly.
The biosynthesis of adenosylcobalamin (vitamin B12).
This review provides the reader with a complete description of the transformation of uroporphyrinogen III into adenosylcobalamin (AdoCbl).
Structural and biochemical characterization of Gun4 suggests a mechanism for its role in chlorophyll biosynthesis.
Kinetic analyses show that Gun4 dramatically increases the efficiency of transformation of porphyrin substrate to metalloporphyr in product and that it also reduces the threshold Mg2+ concentration required for activity at low porphirin concentration, and likely acts as a molecular switch in vivo so that in its absence magnesium chelatase is inactive.
The three-dimensional structure of a Trichoderma reesei beta-mannanase from glycoside hydrolase family 5.
- E. Sabini, H. Schubert, G. Murshudov, K. Wilson, M. Siika‐aho, M. Penttilä
- ChemistryActa crystallographica. Section D, Biological…
The crystal structure of the catalytic core domain of beta-mannanase from the fungus Trichoderma reesei has been determined using the anomalous scattering from a single non-isomorphous platinum complex with two heavy-metal sites in space group P2(1).
Structural and functional studies on the extracellular domain of BST2/tetherin in reduced and oxidized conformations
- H. Schubert, Q. Zhai, C. Hill
- Biology, ChemistryProceedings of the National Academy of Sciences
- 29 September 2010
The data raise the possibility that BST2 may function as a tetramer at some stage, such as during trafficking, and strongly support a model in which the primary functional state of BST2 is a parallel disulfide-bound coiled coil that displays flexibility toward its N terminus.