1N67 Cell Adhesion date Nov 08, 2002
title Clumping Factor A From Staphylococcus Aureus
authors C.C.S.Deivanayagam, E.R.Wann, W.Chen, M.Carson, K.R.Rajashankar, M.Hook, S.V.L.Narayana
compound source
Molecule: Clumping Factor
Chain: A
Engineered: Yes
Organism_scientific: Staphylococcus Aureus
Organism_common: Bacteria
Expression_system: Escherichia Coli
Expression_system_common: Bacteria
symmetry Space Group: P 21 21 21
R_factor 0.206
crystal
cell
length a length b length c angle alpha angle beta angle gamma
38.700 80.540 113.890 90.00 90.00 90.00
method X-Ray Diffractionresolution 1.90 Å
ligand MG enzyme
note 1N67 is a representative structure
similarity Belongs to the serine-aspartate repeat-containing protein (sdr) family.[Gram_pos_anchor]
induction Expressed on cells from both exponential and stationary phases. Up-regulated by sigma-b factor during later growth stages. Sigma-b seems to have a transient enhancing effect on bacterial density in the early stages of infection that it lost during later stages of infection.
subcellular loc. Attached to the cell wall peptidoglycan by an amide bond (potential).
Gene CLFA (S. aureus)
function Promotes bacterial attachment exclusively to the gamma-chain of human fibrinogen. Enhances spleen cell proliferative response in vitro, contributing significantly to the immunostimulatory activity of s.aureus. Cell surface-associated protein implicated in virulence. Significantly decreases macrophage phagocytosis possibly thanks to the clumps, clumped bacteria being too large to be phagocytosed. Dominant factor responsible for human platelet aggregation, which may be an important mechanism for initiating infective endocarditis. Induces formation of bacterial clumps, which diminish the ability of group iia phospholipase a2 to cause bacterial phospholipid hydrolysis and killing.
Gene
Ontology
ChainFunctionProcessComponent
A
  • protein binding
  • cell adhesion
  • pathogenesis
  • cell wall
  • cell surface
  • membrane
  • Primary referenceA 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
    Data retrieval
  • Asymmetric unit, PDB entry: [header only] [complete with coordinates] (63 Kb) [Save to disk]
  • Biological Unit Coordinates (1n67.pdb1.gz) 59 Kb
  • CSU: Contacts of Structural Units for 1N67
  • Likely Quarternary Molecular Structure file(s) for 1N67
  • Structure Factors (268 Kb)
  • Retrieve 1N67 in mmCIF format [Save to disk]
  • View 1N67 in 3D
  • Proteopedia, because life has more than 2D.
  • On Jmol, a nice Rasmol like molecule viewer. This is good for easiest viewing of basic structure.
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  • Structure-derived information
  • Electron Density related parameters from EDS Electron Density Server, at Upsala
  • Dipole moment, from Dipole Server at Weizmann Institute
  • Crystal Contacts, from CryCo at Weizmann Institute
  • 3D motif for 1N67, from MSDmotif at EBI
  • Classification of representative domains in scop (Structural Classification of Proteins)
        - Domain d1n67a1, region A:229-369 [Jmol] [rasmolscript] [script source]
        - Domain d1n67a2, region A:370-560 [Jmol] [rasmolscript] [script source]
  • Fold representative 1n67 from FSSP and Dali (Families of Structurally Similar Proteins)
  • Class (fold), Architecture (subfold), Topology, Homologous superfamily from CATH
  • Summaries and structural analyses of PDB data files from PDBSum
  • Identification of Protein Pockets & Cavities at CASTp
  • Sequence-derived information
  • View one-letter amino acid or nucleotide sequence for each chain: [1n67_A]
  • Other resources with information on 1N67
  • InterPro: IPR001899 , IPR005877
  • PDBREPORT (protein verification by WHAT_CHECK procedures)
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