International
Tables for
Crystallography
Volume F
Crystallography of biological macromolecules
Edited by M. G. Rossmann and E. Arnold

© International Union of Crystallography 2006
International Tables for Crystallography (2006). Vol. F. ch. 1.3, pp. 19-20

Table 1.3.4.3 

W. G. J. Hola* and C. L. M. J. Verlindea

aBiomolecular Structure Center, Department of Biological Structure, Howard Hughes Medical Institute, University of Washington, Seattle, WA 98195-7742, USA
Correspondence e-mail:  hol@gouda.bmsc.washington.edu

Table 1.3.4.3 | top | pdf |
Protein structures of important human pathogenic protozoa, fungi and helminths

(a) Protozoa

Organism Disease Protein structures solved Reference
Acanthamoeba sp. Opportunistic meningoencephalitis, corneal ulcers Actophorin [1]
Profilin [2]
Cryptosporidium parvum Cryptosporidiosis None  
Entamoeba histolytica Amoebic dysentery, liver abscesses None  
Giardia lamblia Giardiasis None  
Leishmania sp. Leishmaniasis Adenine phosphoribosyltransferase [3]
Dihydrofolate reductase-thymidylate synthase [4]
Glyceraldehyde-3-phosphate dehydrogenase [5]
Leishmanolysin [6]
Nucleoside hydrolase [7]
Pyruvate kinase [8]
Triosephosphate isomerase [9]
Plasmodium sp. Malaria Fructose-1,6-bisphosphate aldolase [10]
Lactate dehydrogenase [11]
MSP1 [12]
Plasmepsin II [13]
Purine phosphoribosyltransferase [14]
Triosephosphate isomerase [15]
Pneumocystis carinii Pneumonia Dihydrofolate reductase [16]
Toxoplasma gondii Toxoplasmosis HGXPRTase [17]
UPRTase [18]
Trichomonas vaginalis Trichomoniasis None  
Trypanosoma brucei Sleeping sickness Fructose-1,6-bisphosphate aldolase [19]
Glyceraldehyde-3-phosphate dehydrogenase [20]
6-Phosphogluconate dehydrogenase [21]
Phosphoglycerate kinase [22]
Triosephosphate isomerase [23]
VSG [24]
Trypanosoma cruzi Chagas' disease Cruzain (cruzipain) [25]
Glyceraldehyde-3-phosphate dehydrogenase [26]
Hypoxanthine phosphoribosyltransferase [27]
Triosephosphate isomerase [28]
Trypanothione reductase [29]
Tyrosine aminotransferase [30]

(b) Fungi

Organism Disease Protein structures solved Reference
Aspergillus fumigatus Aspergillosis Restrictocin [31]
Blastomyces dermatidis Blastomycosis None  
Candida albicans Candidiasis Dihydrofolate reductase [32]
N-Myristoyl transferase [33]
Phosphomannose isomerase [34]
Secreted Asp protease [35]
Coccidiodes immitis Coccidioidomycosis None  
Cryptococcus neoformans Cryptococcosis None  
Histoplasma capsulatum Histoplasmosis None  
Mucor sp. Mucormycosis None  
Paracoccidioides brasiliensis Paracoccidioidomycosis None  
Rhizopus sp. Phycomycosis Lipase II [36]
Rhizopuspepsin [37]
RNase Rh [38]

(c) Helminths

Organism Disease Protein structures solved Reference
Clonorchis sinensis Clonorchiasis None  
Fasciola hepatica Fasciolasis Glutathione S-transferase [39]
Fasciolopsis buski Fasciolopsiasis None  
Paragominus westermani Paragonimiasis None  
Schistosoma sp. Schistosomiasis Glutathione S-transferase [39], [40]
Hexokinase [41]
Diphyllobotrium latum Diphyllobothriasis None  
Echinococcus granulosus Unilocular hydatid cyst disease None  
Taenia saginata Taeniasis None  
Taenia solium Taeniasis None  
Ancylostoma duodenale Old World hookworm disease None  
Anisakis Anisakiasis None  
Ascaris lumbricoides Ascariasis Haemoglobin [42]
Major sperm protein [43]
Trypsin inhibitor [44]
Enterobius vermicularis Pinworm infection None  
Necator New World hookworm disease None  
Strongyloides stercoralis Strongyloidiasis None  
Trichinella spiralis Trichinosis None  
Trichuris trichiura Whipworm infection None  
Brugia malayi Filariasis Peptidylprolyl isomerase [45], [46]
Dracunculus medinensis Guinea worm disease None  
Loa loa Loiasis None  
Onchocerca volvulus River blindness None  
Toxocara canis Visceral larva migrans None  
Wuchereria bancrofti Lymphatic filariasis (elephantiasis) None  

References: [1] Leonard et al. (1997)[link]; [2] Liu et al. (1998)[link]; [3] Phillips et al. (1999)[link]; [4] Knighton et al. (1994)[link]; [5] Kim et al. (1995)[link]; [6] Schlagenhauf et al. (1998)[link]; [7] Shi, Schramm & Almo (1999)[link]; [8] Rigden et al. (1999)[link]; [9] Williams et al. (1999)[link]; [10] Kim et al. (1998)[link]; [11] Read et al. (1999)[link]; [12] Chitarra et al. (1999)[link]; [13] Silva et al. (1996)[link]; [14] Shi, Li et al. (1999)[link]; [15] Velanker et al. (1997)[link]; [16] Champness et al. (1994)[link]; [17] Schumacher et al. (1996)[link]; [18] Schumacher et al. (1998)[link]; [19] Chudzik et al. (2000[link]); [20] Vellieux et al. (1993)[link]; [21] Phillips et al. (1998)[link]; [22] Bernstein et al. (1998)[link]; [23] Wierenga et al. (1987)[link]; [24] Freymann et al. (1990)[link]; [25] McGrath et al. (1995)[link]; [26] Souza et al. (1998)[link]; [27] Focia et al. (1998)[link]; [28] Maldonado et al. (1998)[link]; [29] Lantwin et al. (1994)[link]; [30] Blankenfeldt et al. (1999)[link]; [31] Yang & Moffat (1995)[link]; [32] Whitlow et al. (1997)[link]; [33] Weston et al. (1998)[link]; [34] Cleasby et al. (1996)[link]; [35] Cutfield et al. (1995)[link]; [36] Kohno et al. (1996)[link]; [37] Suguna et al. (1987)[link]; [38] Kurihara et al. (1992)[link]; [39] Rossjohn, Feil, Wilce et al. (1997)[link]; [40] McTigue et al. (1995)[link]; [41] Mulichak et al. (1998)[link]; [42] Yang et al. (1995)[link]; [43] Bullock et al. (1996)[link]; [44] Huang et al. (1994)[link]; [45] Mikol et al. (1998)[link]; [46] Taylor et al. (1998)[link].