2E7D

Crystal structure of a NEAT domain from Staphylococcus aureus

Summary for 2E7D

• Entry DOI: 10.2210/pdb2e7d/pdb
• Related: 2H3K 2ITE 2ITF 2O1A
• Descriptor: Hypothetical protein IsdH, SULFATE ION, ACETATE ION, ... (5 entities in total)
• Functional Keywords: ig-like fold, metal binding protein
• Biological source: Staphylococcus aureus
• Cellular location: Secreted, cell wall; Peptidoglycan-anchor (Potential): Q931P4
• Total number of polymer chains: 2
• Total formula weight: 30240.40

Authors

Suenaga, A.,Tanaka, Y.,Yao, M.,Kumagai, I.,Tanaka, I.,Tsumoto, K. (deposition date: 2007-01-09, release date: 2008-01-22, Last modification date: 2024-03-13)

Primary citation

Watanabe, 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

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

Experimental method

X-RAY DIFFRACTION (2.2 Å)