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2XNY

A fragment of streptococcal M1 protein in complex with human fibrinogen

Summary for 2XNY
Entry DOI10.2210/pdb2xny/pdb
Related1BBR 1DUG 1FIB 1FIC 1FID 1FPH 1FZA 1FZB 1FZC 1FZD 1FZE 1FZF 1FZG 1LT9 1LTJ 1N86 1N8E 1RE3 1RE4 1RF0 1RF1 2FFD 2FIB 2VDO 2VDP 2VDQ 2VDR 2VR3 2XNX 2Y7L 3FIB
DescriptorFIBRINOGEN ALPHA CHAIN, FIBRINOGEN BETA CHAIN, FIBRINOGEN GAMMA CHAIN, ... (4 entities in total)
Functional Keywordscell adhesion, virulence factor, streptococcal toxic shock syndrome
Biological sourceSTREPTOCOCCUS PYOGENES
More
Cellular locationSecreted: P02671 P02675 P02679
Secreted, cell wall; Peptidoglycan-anchor (By similarity): Q48WD8
Total number of polymer chains8
Total formula weight192453.31
Authors
Macheboeuf, P.,Y Fu, C.,Zinkernagel, A.S.,Johnson, J.E.,Nizet, V.,Ghosh, P. (deposition date: 2010-08-06, release date: 2011-04-13, Last modification date: 2024-10-16)
Primary citationMacheboeuf, P.,Buffalo, C.,Fu, C.Y.,Zinkernagel, A.S.,Cole, J.N.,Johnson, J.E.,Nizet, V.,Nizet, V.,Ghosh, P.
Streptococcal M1 Protein Constructs a Pathological Host Fibrinogen Network
Nature, 472:64-, 2011
Cited by
PubMed Abstract: M1 protein, a major virulence factor of the leading invasive strain of group A Streptococcus, is sufficient to induce toxic-shock-like vascular leakage and tissue injury. These events are triggered by the formation of a complex between M1 and fibrinogen that, unlike M1 or fibrinogen alone, leads to neutrophil activation. Here we provide a structural explanation for the pathological properties of the complex formed between streptococcal M1 and human fibrinogen. A conformationally dynamic coiled-coil dimer of M1 was found to organize four fibrinogen molecules into a specific cross-like pattern. This pattern supported the construction of a supramolecular network that was required for neutrophil activation but was distinct from a fibrin clot. Disruption of this network into other supramolecular assemblies was not tolerated. These results have bearing on the pathophysiology of streptococcal toxic shock.
PubMed: 21475196
DOI: 10.1038/NATURE09967
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (7.5 Å)
Structure validation

226707

数据于2024-10-30公开中

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