2ln7 | pdb_00002ln7

Backbone 1H, 13C, and 15N Chemical Shift Assignments for the catalytic domain of B. anthracis SrtD

spinqualitylabelsall models 2ln7, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2ln7 is a 1 chain structure with sequence from "bacillus_cereus_var._anthracis"_(cohn_1872)_smith_et_al._1946 "bacillus cereus var. anthracis" (cohn 1872) smith et al. 1946. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: BA_5069, GBAA_5069 ("Bacillus cereus var. anthracis" (Cohn 1872) Smith et al. 1946) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Bacillus anthracis forms metabolically dormant endospores that upon germination can cause lethal anthrax disease in humans. Efficient sporulation requires the activity of the SrtC sortase (BaSrtC), a cysteine transpeptidase that covalently attaches the BasH and BasI proteins to the peptidoglycan of the forespore and predivisional cell, respectively. To gain insight into the molecular basis of protein display, we used nuclear magnetic resonance to determine the structure and backbone dynamics of the catalytic domain of BaSrtC (residues Ser(56)-Lys(198)). The backbone and heavy atom coordinates of structurally ordered amino acids have coordinate precision of 0.42 +/- 0.07 and 0.82 +/- 0.05 A, respectively. BaSrtC(Delta55) adopts an eight-stranded beta-barrel fold that contains two short helices positioned on opposite sides of the protein. Surprisingly, the protein dimerizes and contains an extensive, structurally disordered surface that is positioned adjacent to the active site. The surface is formed by two loops (beta2-beta3 and beta4-H1 loops) that surround the active site histidine, suggesting that they may play a key role in associating BaSrtC with its lipid II substrate. BaSrtC anchors proteins bearing a noncanonical LPNTA sorting signal. Modeling studies suggest that the enzyme recognizes this substrate using a rigid binding pocket and reveals the presence of a conserved subsite for the signal. This first structure of a class D member of the sortase superfamily unveils class-specific features that may facilitate ongoing efforts to discover sortase inhibitors for the treatment of bacterial infections. Solution Structure of the Sortase Required for Efficient Production of Infectious Bacillus anthracis Spores.,Robson SA, Jacobitz AW, Phillips ML, Clubb RT Biochemistry. 2012 Oct 9;51(40):7953-63. doi: 10.1021/bi300867t. Epub 2012 Sep, 27. PMID:22974341 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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