In silico identification and analysis of the binding site for aminocoumarin type inhibitors in the C-terminal domain of Hsp90.

Hsp90 contains two Nucleotide Binding Sites (NBS): one each in its N-terminal domain (NTD) and C-terminal domain (CTD), respectively. Previously we used computational techniques to locate a nucleotide-binding site in the CTD. Nucleotide binding at this site stabilized the structurally labile region within this domain, thus providing a rationale for increased resistance to thermal denaturation and proteolysis.

In silico identification and computational analysis of the nucleotide binding site in the C-terminal domain of Hsp90.

Hsp90 contains two distinct Nucleotide Binding Sites (NBS), in its N-terminal domain (NTD) and C-terminal domain (CTD), respectively. The NTD site belongs to the GHKL super-family of ATPases and has been the subject of extensive characterization. However, a structure of the nucleotide-bound form of CTD is still unavailable.

Fungal cobalamin-independent methionine synthase: Insights from the model organism, Neurospora crassa.

Two families of methionine synthases, distinct in catalytic and structural features, have been encountered: MetH, the cobalamin-dependent enzyme and MetE, the cobalamin-independent form. The MetE family is of mechanistic interest due to the chemically challenging nature of the reaction and is a potential target for antifungal therapeutics since the human genome encodes only MetH. Here we report the identification, purification, and crystal structure of MetE from the filamentous fungus Neurospora crassa (ncMetE).

Homology modeling, ligand docking and in silico mutagenesis of neurospora Hsp80 (90): insight into intrinsic ATPase activity.

The Hsp90 family of proteins is an important component of the cellular response to elevated temperatures, environmental or physiological stress and nuclear receptor signalling. The primary object of this work is the 80-kDa heat shock protein, a member of the Hsp90 family, from the model filamentous fungus Neurospora crassa, (henceforth referred to as Hsp80Nc). In contrast to more extensively characterized members of the same family, (e.