4FYC

Structural and functional characterizations of a thioredoxin-fold protein from Helicobacter pylori

Summary for 4FYC

• Entry DOI: 10.2210/pdb4fyc/pdb
• Related: 4FYB
• Descriptor: Thiol:disulfide interchange protein (DsbC), TETRAETHYLENE GLYCOL (3 entities in total)
• Functional Keywords: thioredoxin fold, reductase, oxidoreductase
• Biological source: Helicobacter pylori
• Total number of polymer chains: 2
• Total formula weight: 55290.53

Authors

Yoon, J.Y.,Kim, J.,Lee, S.J.,Im, H.N.,Kim, H.S.,Yoon, H.,An, D.R.,Kim, J.Y.,Kim, S.,Han, B.W.,Suh, S.W. (deposition date: 2012-07-04, release date: 2013-05-08, Last modification date: 2023-11-08)

Primary citation

Yoon, J.Y.,Kim, J.,An, D.R.,Lee, S.J.,Kim, H.S.,Im, H.N.,Yoon, H.J.,Kim, J.Y.,Kim, S.J.,Han, B.W.,Suh, S.W.
Structural and functional characterization of HP0377, a thioredoxin-fold protein from Helicobacter pylori
Acta Crystallogr.,Sect.D, 69:735-746, 2013

PubMed 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.

PubMed: 23633582
DOI: 10.1107/S0907444913001236

Experimental method

X-RAY DIFFRACTION (2.31 Å)