4udm

Crystal structure of Im3 in complex with Y52A mutant of E3RNase

spinqualitylabelsall models 4udm, resolution 2.96Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4udm is a 2 chain structure with sequence from Ecobd. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, CL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [IMM3_ECOLX] This protein inhibits the 16S RNA hydrolyzing activity of colicin E3 by binding with high affinity to the C-terminal catalytic domain of E3. This protein is able to protect a cell, which harbors the plasmid ColE3 against colicin E3. [CEA3_ECOLX] Inactivates ribosomes by hydrolyzing 16S RNA in 30S ribosomes at a specific site. Colicins are polypeptide toxins produced by and active against E.coli and closely related bacteria. Publication Abstract from PubMed The kinetic and thermodynamic consequences of intrinsic disorder in protein-protein recognition are controversial. We address this by inducing one partner of the high-affinity colicin E3 rRNase domain-Im3 complex (K(d) approximately 10(-12) M) to become an intrinsically disordered protein (IDP). Through a variety of biophysical measurements, we show that a single alanine mutation at Tyr507 within the hydrophobic core of the isolated colicin E3 rRNase domain causes the enzyme to become an IDP (E3 rRNase(IDP)). E3 rRNase(IDP) binds stoichiometrically to Im3 and forms a structure that is essentially identical to the wild-type complex. However, binding of E3 rRNase(IDP) to Im3 is 4 orders of magnitude weaker than that of the folded rRNase, with thermodynamic parameters reflecting the disorder-to-order transition on forming the complex. Critically, pre-steady-state kinetic analysis of the E3 rRNase(IDP)-Im3 complex demonstrates that the decrease in affinity is mostly accounted for by a drop in the electrostatically steered association rate. Our study shows that, notwithstanding the advantages intrinsic disorder brings to biological systems, this can come at severe kinetic and thermodynamic cost. Consequences of inducing intrinsic disorder in a high-affinity protein-protein interaction.,Papadakos G, Sharma A, Lancaster LE, Bowen R, Kaminska R, Leech AP, Walker D, Redfield C, Kleanthous C J Am Chem Soc. 2015 Apr 29;137(16):5252-5. doi: 10.1021/ja512607r. Epub 2015 Apr , 17. PMID:25856265 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Colicin 3D structures Colicin immunity protein 3D structures

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