3FWT

Crystal structure of Leishmania major MIF2

Summary for 3FWT

• Entry DOI: 10.2210/pdb3fwt/pdb
• Related: 3FWU
• Descriptor: Macrophage migration inhibitory factor-like protein (2 entities in total)
• Functional Keywords: homotrimer, tautomerase, cytokine
• Biological source: Leishmania major
• Total number of polymer chains: 1
• Total formula weight: 14769.77

Authors

Walkinshaw, M.D.,Richardson, J.M. (deposition date: 2009-01-19, release date: 2009-03-17, Last modification date: 2023-09-06)

Primary citation

Richardson, J.M.,Morrison, L.S.,Bland, N.D.,Bruce, S.,Coombs, G.H.,Mottram, J.C.,Walkinshaw, M.D.
Structures of Leishmania major orthologues of macrophage migration inhibitory factor
Biochem.Biophys.Res.Commun., 380:442-448, 2009

PubMed Abstract: Leishmania major, an intracellular parasitic protozoon that infects, differentiates and replicates within macrophages, expresses two closely related MIF-like proteins. To ascertain the roles and potential differences of these two Leishmania proteins, recombinant L. major MIF1 and MIF2 have been produced and the structures resolved by X-ray crystallography. Each has a trimeric ring architecture similar to mammalian MIF, but with some structurally distinct features. LmjMIF1, but not LmjMIF2, has tautomerase activity. LmjMIF2 is found in all life cycle stages whereas LmjMIF1 is found exclusively in amastigotes, the intracellular stage responsible for mammalian disease. The findings are consistent with parasite MIFs modulating or circumventing the host macrophage response, thereby promoting parasite survival, but suggest the LmjMIFs have potentially different biological roles. Analysis of the Leishmania braziliensis genome showed that this species lacks both MIF genes. Thus MIF is not a virulence factor in all species of Leishmania.

PubMed: 19187777
DOI: 10.1016/j.bbrc.2009.01.030

Experimental method

X-RAY DIFFRACTION (1.9 Å)