6E95
Chimeric structure of Saccharomyces cerevisiae GCN4 leucine zipper fused to Staphylococcus aureus AgrC cytoplasmic histidine kinase module (dataset isotropically truncated by HKL2000)
Summary for 6E95
| Entry DOI | 10.2210/pdb6e95/pdb |
| Related | 6E52 |
| Descriptor | Staphylococcus aureus AgrC histidine kinase module fused to Saccharomyces cerevisiae GCN4 leucine zipper (2 entities in total) |
| Functional Keywords | protein histidine kinase, bacterial quorum sensing, coiled coil, bergerat fold, signaling protein |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) More |
| Total number of polymer chains | 2 |
| Total formula weight | 57687.74 |
| Authors | Xie, Q.,Jeffrey, P.D.,Muir, T.W. (deposition date: 2018-07-31, release date: 2019-02-27, Last modification date: 2024-03-13) |
| Primary citation | Xie, Q.,Zhao, A.,Jeffrey, P.D.,Kim, M.K.,Bassler, B.L.,Stone, H.A.,Novick, R.P.,Muir, T.W. Identification of a Molecular Latch that Regulates Staphylococcal Virulence. Cell Chem Biol, 26:548-558.e4, 2019 Cited by PubMed Abstract: Virulence induction in the Staphylococcus aureus is under the control of a quorum sensing (QS) circuit encoded by the accessory gene regulator (agr) locus. Allelic variation within agr produces four QS specificity groups, each producing a unique secreted autoinducer peptide (AIP) and receptor histidine kinase (RHK), AgrC. Cognate AIP-AgrC interactions activate virulence through a two-component signaling cascade, whereas non-cognate pairs are generally inhibitory. Here we pinpoint a key hydrogen-bonding interaction within AgrC that acts as a switch to convert helical motions propagating from the receptor sensor domain into changes in inter-domain association within the kinase module. AgrC mutants lacking this interaction are constitutively active in vitro and in vivo, the latter leading to a pronounced attenuation of S. aureus biofilm formation. Thus, our work sheds light on the regulation of this biomedically important RHK. PubMed: 30773482DOI: 10.1016/j.chembiol.2019.01.006 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.25 Å) |
Structure validation
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