Structural basis for multimeric heme complexation through a specific protein-heme interaction: The case of the third NEAT domain of IsdH from Staphylococcus aureus

Masato Watanabe, Yoshikazu Tanaka, Ayuko Suenaga, Makoto Kuroda, Min Yao, Nobuhisa Watanabe, Fumio Arisaka, Toshiko Ohta, Isao Tanaka, Kouhei Tsumoto

Research output: Contribution to journalArticlepeer-review

68 Citations (Scopus)

Abstract

To elucidate the heme acquisition system in pathogenic bacteria, we investigated the heme-binding properties of the third NEAT domain of IsdH (IsdH-NEAT3), a receptor for heme located on the surfaces of pathogenic bacterial cells, by using x-ray crystallography, isothermal titration calorimetry, examination of absorbance spectra, mutation analysis, size-exclusion chromatography, and analytical ultracentrifugation. We found the following: 1) IsdH-NEAT3 can bind with multiple heme molecules by two modes; 2) heme was bound at the surface of IsdH-NEAT3; 3) candidate residues proposed from the crystal structure were not essential for binding with heme; and 4) IsdHNEAT3 was associated into a multimeric heme complex by the addition of excess heme. From these observations, we propose a heme-binding mechanism for IsdH-NEAT3 that involves multimerization and discuss the biological importance of this mechanism.

Original languageEnglish
Pages (from-to)28649-28659
Number of pages11
JournalJournal of Biological Chemistry
Volume283
Issue number42
DOIs
Publication statusPublished - 2008 Oct 17

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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