1YZV

HYPOTHETICAL PROTEIN FROM TRYPANOSOMA CRUZI

1YZV の概要

• エントリーDOI: 10.2210/pdb1yzv/pdb
• 分子名称: HYPOTHETICAL PROTEIN, SULFATE ION (3 entities in total)
• 機能のキーワード: structural genomics, psi, protein structure initiative, structural genomics of pathogenic protozoa consortium, sgpp, unknown function
• 由来する生物種: Trypanosoma cruzi
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 22657.40

構造登録者

Caruthers, J.,Merritt, E.A.,Structural Genomics of Pathogenic Protozoa Consortium (SGPP) (登録日: 2005-02-28, 公開日: 2005-03-08, 最終更新日: 2024-02-14)

主引用文献

Caruthers, J.,Zucker, F.,Worthey, E.,Myler, P.J.,Buckner, F.,Van Voorhuis, W.,Mehlin, C.,Boni, E.,Feist, T.,Luft, J.,Gulde, S.,Lauricella, A.,Kaluzhniy, O.,Anderson, L.,Le Trong, I.,Holmes, M.A.,Earnest, T.,Soltis, M.,Hodgson, K.O.,Hol, W.G.,Merritt, E.A.
Crystal structures and proposed structural/functional classification of three protozoan proteins from the isochorismatase superfamily.
Protein Sci., 14:2887-2894, 2005

PubMed Abstract: We have determined the crystal structures of three homologous proteins from the pathogenic protozoans Leishmania donovani, Leishmania major, and Trypanosoma cruzi. We propose that these proteins represent a new subfamily within the isochorismatase superfamily (CDD classification cd004310). Their overall fold and key active site residues are structurally homologous both to the biochemically well-characterized N-carbamoylsarcosine-amidohydrolase, a cysteine hydrolase, and to the phenazine biosynthesis protein PHZD (isochorismase), an aspartyl hydrolase. All three proteins are annotated as mitochondrial-associated ribonuclease Mar1, based on a previous characterization of the homologous protein from L. tarentolae. This would constitute a new enzymatic activity for this structural superfamily, but this is not strongly supported by the observed structures. In these protozoan proteins, the extended active site is formed by inter-subunit association within a tetramer, which implies a distinct evolutionary history and substrate specificity from the previously characterized members of the isochorismatase superfamily. The characterization of the active site is supported crystallographically by the presence of an unidentified ligand bound at the active site cysteine of the T. cruzi structure.

PubMed: 16199669
DOI: 10.1110/ps.051783005

実験手法

X-RAY DIFFRACTION (2.001 Å)