4yxj

Structure of Thermotoga maritima DisA in complex with ApCpp

spinqualitylabelsall models 4yxj, resolution 2.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4yxj is a 2 chain structure with sequence from Thermotoga maritima. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.55Å Ligands: APC Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function DISA_THEMA Participates in a DNA-damage check-point. DisA forms globular foci that rapidly scan along the chromosomes searching for lesions (By similarity). Has also diadenylate cyclase activity, catalyzing the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP). c-di-AMP likely acts as a signaling molecule that may couple DNA integrity with a cellular process. Does not convert GTP to c-di-GMP. Publication Abstract from PubMed The identification of the essential bacterial second messenger cyclic-di-AMP synthesized by the DNA-integrity scanning protein DisA opened up a new and emerging field in bacterial signaling. To further analyze the di-adenylate cyclase reaction catalyzed by the DAC domains of DisA, we crystallized Thermotoga maritima DisA in presence of different ATP analogs and metal ions to identify the metal binding site and trap the enzyme in pre- and post-reaction states. Through structural and biochemical assays we identified important residues essential for the reaction in the active site of the DAC domains. Our structures resolve the metal binding site and thus explain the activation of ATP for the DAC reaction. Moreover, we were able to identify a potent inhibitor of the DAC domain. Based on the available structures and homology to annotated DAC domains we propose a common mechanism for c-di-AMP synthesis by DAC domains in c-di-AMP producing species and a possible approach for its effective inhibition. Structural analysis of the di-adenylate cyclase reaction of DNA-integrity scanning protein A (DisA) and its inhibition by 3'-dATP.,Muller M, Deimling T, Hopfner KP, Witte G Biochem J. 2015 May 27. PMID:26014055 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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