2odm

Crystal structure of S. aureus YlaN, an essential leucine rich protein involved in the control of cell shape

spinqualitylabelsall models 2odm, resolution 2.24Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2odm is a 2 chain structure with sequence from Staaw. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: MSE Gene: ylaN (STAAW) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The crystal structure of a conserved leucine rich protein, YlaN, from Staphylococcus aureus has been determined by X-ray crystallography to 2.3 A resolution. Whilst the precise function of S. aureus YlaN is unknown its homologue in B. subtilis has been shown to be essential for cell survival and is thought to be involved in controlling cell shape. The structure of S. aureus YlaN provides the first view of its protein family, which reveals that it is a novel homodimer whose subunit architecture is comprised of an antiparallel 3 helix bundle reminiscent of the helical arrangements seen in leucine zipper proteins. Analysis of the pattern of sequence conservation on the structure has led to the identification of two connected solvent exposed patches of conserved residues in each subunit located at one end of but on opposite faces of the molecule. We suggest that YlaN has a binding role in the cell rather than a catalytic function and a search for its ligand is underway to accelerate its exploitation as a target for antibiotic discovery. Crystal structure of S. aureus YlaN, an essential leucine rich protein involved in the control of cell shape.,Xu L, Sedelnikova SE, Baker PJ, Hunt A, Errington J, Rice DW Proteins. 2007 Aug 1;68(2):438-45. PMID:17469204 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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