5ahw

Crystal structure of universal stress protein MSMEG_3811 in complex with cAMP

spinqualitylabelsall models 5ahw, resolution 2.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ahw is a 6 chain structure with sequence from Mycolicibacterium smegmatis MC2 155. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.15Å Ligands: CL, CMP, POG, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0QYW6_MYCS2 Publication Abstract from PubMed Mycobacteria are endowed with rich and diverse machinery for the synthesis, utilization and degradation of cAMP. The actions of cyclic nucleotides are generally mediated by binding of cAMP to conserved and well-characterized cyclic nucleotide binding (CNB) domains, or structurally distinct GAF domain-containing proteins. Proteins with CNB and GAF domains can be identified in the genome of Mycobacterial species and some of them have been characterized. Here we show that a significant fraction of intracellular cAMP is bound to protein in Mycobacterial species, and using affinity chromatography techniques, identify specific universal stress proteins (USP) as abundantly expressed cAMP-binding proteins in slow-growing as well as fast growing Mycobacteria. We have characterized the biochemical and thermodynamic parameters for binding of cAMP, and show that these USPs bind cAMP with a higher affinity than ATP, an established ligand for other USPs. We determined the structure of the USP MSMEG_3811 bound to cAMP and confirmed through structure guided mutagenesis residues important for cAMP binding. This family of USPs is conserved in all Mycobacteria and we suggest that they serve as 'sinks' for cAMP, making this second messenger available for downstream effectors as and when ATP levels are altered in the cell. A Universal Stress Protein (USP) in Mycobacteria binds cAMP.,Banerjee A, Adolph RS, Gopalakrishnapai J, Kleinboelting S, Emmerich C, Steegborn C, Visweswariah SS J Biol Chem. 2015 Mar 23. pii: jbc.M115.644856. PMID:25802331 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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