Acta Crystallographica Section D

Biological Crystallography

Volume 69, Part 5 (May 2013)


research papers



Acta Cryst. (2013). D69, 735-746    [ doi:10.1107/S0907444913001236 ]

Structural and functional characterization of HP0377, a thioredoxin-fold protein from Helicobacter pylori

J. Y. Yoon, J. Kim, D. R. An, S. J. Lee, H. S. Kim, H. N. Im, H.-J. Yoon, J. Y. Kim, S.-J. Kim, B. W. Han and S. W. Suh

Abstract: Maturation of cytochrome c is carried out in the bacterial periplasm, where specialized thiol-disulfide oxidoreductases provide the correct reduction of oxidized apocytochrome c before covalent haem attachment. HP0377 from Helicobacter pylori is a thioredoxin-fold protein that has been implicated as a component of system II for cytochrome c assembly and shows limited sequence similarity to Escherichia coli DsbC, a disulfide-bond isomerase. To better understand the role of HP0377, its crystal structures have been determined in both reduced and partially oxidized states, which are highly similar to each other. Sedimentation-equilibrium experiments indicate that HP0377 is monomeric in solution. HP0377 adopts a thioredoxin fold but shows distinctive variations as in other thioredoxin-like bacterial periplasmic proteins. The active site of HP0377 closely resembles that of E. coli DsbC. A reductase assay suggests that HP0377 may play a role as a reductase in the biogenesis of holocytochrome c553 (HP1227). Binding experiments indicate that it can form a covalent complex with HP0518, a putative L,D-transpeptidase with a catalytic cysteine residue, via a disulfide bond. Furthermore, physicochemical properties of HP0377 and its R86A variant have been determined. These results suggest that HP0377 may perform multiple functions as a reductase in H. pylori.

PDB references: 4fyb and 4fyc

Keywords: cytochrome c biogenesis; DsbC; Helicobacter pylori; HP0377; HP0518; HP1227.


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