3tcj | pdb_00003tcj

CcdB dimer from V. fisheri in complex with one C-terminal domain of F-plasmid CcdA

spinqualitylabelsall models 3tcj, resolution 1.93Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3tcj is a 3 chain structure with sequence from "achromobacter_fischeri"_(beijerinck_1889)_bergey_et_al._1930 "achromobacter fischeri" (beijerinck 1889) bergey et al. 1930. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACT Related: 3jrz, 3jsc, 3ku8, 3kua, 3hpw, 3g7f Gene: ccdB ("Achromobacter fischeri" (Beijerinck 1889) Bergey et al. 1930) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CCDA_ECO57] Antitoxin component of a toxin-antitoxin (TA) module which inhibits the post-segregational killing (PSK) of plasmid-free cells, also referred to as a plasmid addiction system. Binds to and blocks the activity of CcdB; will also remove bound CcdB protein from the CcdB-GyrA complex by forming a CcdA-CcdB complex, a process termed rejuvenation. Functions as a transcriptional corepressor for the ccdAB operon, repression also requires CcdB (By similarity). Publication Abstract from PubMed Intrinsically disordered proteins (IDPs) are proteins that lack a unique three-dimensional structure in their native state. Many have, however, been found to fold into a defined structure when interacting with specific binding partners. The energetic implications of such behavior have been widely discussed, yet experimental thermodynamic data is scarce. We present here a thorough thermodynamic and structural study of the binding of an IDP (antitoxin CcdA) to its molecular target (gyrase poison CcdB). We show that the binding-coupled folding of CcdA is driven by a combination of specific intramolecular interactions that favor the final folded structure and a less specific set of intermolecular contacts that provide a desolvation entropy boost. The folded structure of the bound IDP appears to be defined largely by its own amino acid sequence, with the binding partner functioning more as a facilitator than a mold to conform to. On the other hand, specific intermolecular interactions do increase the binding affinity up to the picomolar range. Overall, this study shows how an IDP can achieve very strong and structurally well-defined binding and it provides significant insight into the molecular forces that enable such binding properties. Energetic basis of uncoupling folding from binding for an intrinsically disordered protein.,Drobnak I, De Jonge N, Haesaerts S, Vesnaver G, Loris R, Lah J J Am Chem Soc. 2013 Jan 30;135(4):1288-94. doi: 10.1021/ja305081b. Epub 2013 Jan , 16. PMID:23289531 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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