Crystallization and Preliminary X-Ray Crystallographic Analysis of Plasmodium Falciparum S-Adenosyl-L-Homocysteine Hydrolase

Authors: Tanaka, Nobutada; Kusakabe, Yoshio; Shiraiwa, Katsura; Sakamoto, Yasumitsu; Nakanishi, Masayuki; Kitade, Yukio; Nakamura, Kazuo T.

Source: Protein and Peptide Letters, Volume 11, Number 2, April 2004 , pp. 201-205(5)

Publisher: Bentham Science Publishers

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Abstract:

S-adenosyl-L-homocysteine hydrolase from a malaria parasite Plasmodium falciparum (PfSAHH) has been crystallized by the vapor diffusion method. The crystals belong to an orthorhombic space group P212121 with the cell dimensions of a = 76.66 Å, b = 86.31 Å, and c = 335.6 Å. There are four subunits (one tetramer) per asymmetric unit. X-ray diffraction data have been collected up to 2.8 Å resolution. Selfrotation function studies suggest that the tetrameric PfSAHH molecule has the 222 point group symmetry.

Keywords: Plasmodium; S-adenosyl-L-homocysteine; hydrolase; orthorhombic

Document Type: Review Article

DOI: http://dx.doi.org/10.2174/0929866043478248

Affiliations: School of Pharmaceutical Sciences, Showa University, Tokyo 142-8555, JAPAN.

Publication date: April 1, 2004

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.

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