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2Z6F

Crystal structure of NEAT domain from Staphylococcus aureus in complex with heme

Summary for 2Z6F
Entry DOI10.2210/pdb2z6f/pdb
Related2E7D 2H3K 2ITE 2ITF 2O1A 2O6P
DescriptorIron-regulated surface determinant protein H, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
Functional Keywordsigg-like fold, cell wall, peptidoglycan-anchor, secreted, heme binding protein
Biological sourceStaphylococcus aureus
Cellular locationSecreted, cell wall; Peptidoglycan-anchor (Potential): Q931P4
Total number of polymer chains1
Total formula weight15470.98
Authors
Tanaka, Y.,Suenaga, A.,Tsumoto, K. (deposition date: 2007-07-31, release date: 2008-07-29, Last modification date: 2023-11-01)
Primary citationWatanabe, M.,Tanaka, Y.,Suenaga, A.,Kuroda, M.,Yao, M.,Watanabe, N.,Arisaka, F.,Ohta, T.,Tanaka, I.,Tsumoto, K.
Structural basis for multimeric heme complexation through a specific protein-heme interaction: the case of the third neat domain of IsdH from Staphylococcus aureus
J.Biol.Chem., 283:28649-28659, 2008
Cited by
PubMed 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) IsdH-NEAT3 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.
PubMed: 18667422
DOI: 10.1074/jbc.M803383200
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

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