2l0r | pdb_00002l0r

Conformational Dynamics of the Anthrax Lethal Factor Catalytic Center

spinqualitylabelsall models 2l0r, 31 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2l0r 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: BXA0172, GBAA_pXO1_0172, lef, pXO1-107 ("Bacillus cereus var. anthracis" (Cohn 1872) Smith et al. 1946) Activity: Hydrolase, with EC number 3.4.24.83 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [LEF_BACAN] One of the three proteins composing the anthrax toxin, the agent which infects many mammalian species and that may cause death. LF is the lethal factor that, when associated with PA, causes death. LF is not toxic by itself. It is a protease that cleaves the N-terminal of most dual specificity mitogen-activated protein kinase kinases (MAPKKs or MAP2Ks) (except for MAP2K5). Cleavage invariably occurs within the N-terminal proline-rich region preceding the kinase domain, thus disrupting a sequence involved in directing specific protein-protein interactions necessary for the assembly of signaling complexes. There may be other cytosolic targets of LF involved in cytotoxicity. The proteasome may mediate a toxic process initiated by LF in the cell cytosol involving degradation of unidentified molecules that are essential for macrophage homeostasis. This is an early step in LeTx intoxication, but it is downstream of the cleavage by LF of MEK1 or other putative substrates. Publication Abstract from PubMed Anthrax lethal factor (LF) is a zinc-metalloprotease that together with the protective antigen constitutes anthrax lethal toxin, which is the most prominent virulence factor of the anthrax disease. The solution nuclear magnetic resonance and in silico conformational dynamics of the 105 C-terminal residues of the LF catalytic core domain in its apo form are described here. The polypeptide adopts a compact structure even in the absence of the Zn(2+) cofactor, while the 40 N-terminal residues comprising the metal ligands and residues that participate in substrate and inhibitor recognition exhibit more flexibility than the C-terminal region. Conformational dynamics of the anthrax lethal factor catalytic center.,Dalkas GA, Chasapis CT, Gkazonis PV, Bentrop D, Spyroulias GA Biochemistry. 2010 Dec 28;49(51):10767-9. Epub 2010 Dec 3. PMID:21121613 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Anthrax Lethal Factor

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