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 Diffraction	resolution	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	Chain Function Process Component A protein binding cell adhesion pathogenesis cell wall cell surface membrane
Primary 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

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

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Visual 3D analysis of 1N67

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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) MMDB (Entrez's Structure Database)

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