1N67

Clumping Factor A from Staphylococcus aureus

Summary for 1N67

• Entry DOI: 10.2210/pdb1n67/pdb
• Related: 1AMX
• Descriptor: Clumping Factor, MAGNESIUM ION (3 entities in total)
• Functional Keywords: dev-igg, igg, immunoglobulin, igsf, clumping factor, staphylococcus aureus, fibrinongen-binding, cell adhesion
• Biological source: Staphylococcus aureus
• Cellular location: Secreted, cell wall ; Peptidoglycan-anchor : Q53653
• Total number of polymer chains: 1
• Total formula weight: 39010.79

Authors

Deivanayagam, C.C.S.,Wann, E.R.,Chen, W.,Carson, M.,Rajashankar, K.R.,Hook, M.,Narayana, S.V.L. (deposition date: 2002-11-08, release date: 2003-03-04, Last modification date: 2024-02-14)

Primary citation

Deivanayagam, C.C.S.,Wann, E.R.,Chen, W.,Carson, M.,Rajashankar, K.R.,Hook, M.,Narayana, S.V.L.
A novel variant of the immunoglobulin fold in surface adhesins of Staphylococcus aureus: crystal structure of the fibrinogen-binding MSCRAMM, clumping factor A
Embo J., 21:6660-6672, 2002

PubMed Abstract: 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.

PubMed: 12485987
DOI: 10.1093/emboj/cdf619

Experimental method

X-RAY DIFFRACTION (1.9 Å)