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Identification and Tetramer Structure of SPD_0310 Hemin-storage Protein Linked to Streptococcus pneumoniae Iron Homeostasis and Virulence

ABSTRACT: We found that the homologous proteins of SPD_0310 of Streptococcus pneumoniae widely exists in Gram-positive bacteria. SPD_0310 has heme binding ability. In the GST pull-down experiment, we found that it can interact with several proteins.

INSTRUMENT(S): TripleTOF 5600

ORGANISM(S): Streptococcus Pneumoniae Serotype 2 (strain D39 / Nctc 7466)

SUBMITTER: Kun Cao

LAB HEAD: Institute of Life and Health Engineering, College of Life Science and Technology

PROVIDER: PXD030298 | Pride | 2022-08-12

REPOSITORIES: Pride

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			Action	DRS
	CK20131231_102.mgf	Mgf
	CK_20131205_101.RAW	Raw
	CK_20131205_101.mgf	Mgf
	CK_20131205_102.RAW	Raw
	CK_20131205_103.RAW	Raw

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Publications

Identification and Tetramer Structure of Hemin-Binding Protein SPD_0310 Linked to Iron Homeostasis and Virulence of Streptococcus pneumoniae.

Cao Kun K Zhang Tianlong T Li Nan N Yang Xiao-Yan XY Ding Jianping J He Qing-Yu QY Sun Xuesong X

mSystems 20220413 3

Iron and iron-containing compounds are essential for bacterial virulence and host infection. Hemin is an important supplement compound for bacterial survival in an iron-deficient environment. Despite strong interest in hemin metabolism, the detailed mechanism of hemin transportation in Gram-positive bacteria is yet to be reported. The results of our study revealed that the homologous proteins of SPD_0310 were significantly conservative in Gram-positive bacteria (<i>P < </i>0.001), and these prot ...[more]

PMID: 35414267

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