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spinqualitylabelsall models 1n67, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Clumping Factor A from Staphylococcus aureus

Overview

We report here the crystal structure of the minimal ligand-binding segment, of the Staphylococcus aureus MSCRAMM, clumping factor A. This, fibrinogen-binding segment contains two similarly folded domains. The fold, observed is a new variant of the immunoglobulin motif that we have called, DE-variant or the DEv-IgG fold. This subgroup includes the ligand-binding, domain of the collagen-binding S.aureus MSCRAMM CNA, and many other, structures previously classified as jelly rolls. Structure predictions, suggest that the four fibrinogen-binding S.aureus MSCRAMMs identified so, far would also contain the same DEv-IgG fold. A systematic docking search, using the C-terminal region of the fibrinogen gamma-chain as a probe, suggested that a hydrophobic pocket formed between the two DEv-IgG domains, of the clumping factor as the ligand-binding site. Mutagenic substitution, of residues Tyr256, Pro336, Tyr338 and Lys389 in the clumping factor, which are proposed to contact the terminal residues (408)AGDV(411) of the, gamma-chain, resulted in proteins with no or markedly reduced affinity for, fibrinogen.

About this Structure

1N67 is a Single protein structure of sequence from Staphylococcus aureus with MG as ligand. Full crystallographic information is available from OCA.

Reference

A novel variant of the immunoglobulin fold in surface adhesins of Staphylococcus aureus: crystal structure of the fibrinogen-binding MSCRAMM, clumping factor A., Deivanayagam CC, Wann ER, Chen W, Carson M, Rajashankar KR, Hook M, Narayana SV, EMBO J. 2002 Dec 16;21(24):6660-72. PMID:12485987

Page seeded by OCA on Tue Nov 20 21:59:49 2007