4yjm

The apo structure of Agrobacterium tumefaciens ClpS2

spinqualitylabelsall models 4yjm, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4yjm is a 4 chain structure with sequence from Agrfc. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 4yka, 4yjx Gene: clpS2, Atu2232, AGR_C_4060 (AGRFC) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CLPS2_AGRFC] Involved in the modulation of the specificity of the ClpAP-mediated ATP-dependent protein degradation. Publication Abstract from PubMed The N-end rule dictates that a protein's N-terminal residue determines its half-life. In bacteria, the ClpS adaptor mediates N-end-rule degradation, by recognizing proteins bearing specific N-terminal residues and delivering them to the ClpAP AAA+ protease. Unlike most bacterial clades, many alpha-proteobacteria encode two ClpS paralogs, ClpS1 and ClpS2. Here, we demonstrate that both ClpS1 and ClpS2 from A. tumefaciens deliver N-end-rule substrates to ClpA, but ClpS2 has more stringent binding specificity, recognizing only a subset of the canonical bacterial N-end-rule residues. The basis of this enhanced specificity is addressed by crystal structures of ClpS2, with and without ligand, and structure-guided mutagenesis, revealing protein conformational changes and remodeling in the substrate-binding pocket. We find that ClpS1 and ClpS2 are differentially expressed during growth in A. tumefaciens and conclude that the use of multiple ClpS paralogs allows fine-tuning of N-end-rule degradation at the level of substrate recognition. Structural Basis of an N-Degron Adaptor with More Stringent Specificity.,Stein BJ, Grant RA, Sauer RT, Baker TA Structure. 2016 Jan 20. pii: S0969-2126(15)00534-1. doi:, 10.1016/j.str.2015.12.008. PMID:26805523 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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