3e76

Crystal structure of Wild-type GroEL with bound Thallium ions

spinqualitylabelsall models 3e76, resolution 3.94Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3e76 is a 14 chain structure with sequence from Escherichia coli uti89. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: AGS, MG, TL Related: 2nwc, 1xck, 1kp8 Gene: groL, groEL, UTI89_C4741 (Escherichia coli UTI89) Activity: Chaperonin ATPase, with EC number 3.6.4.9 Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed GroEL is a bacterial chaperone protein that assembles into a homotetradecameric complex exhibiting D(7) symmetry and utilizes the co-chaperone protein GroES and ATP hydrolysis to assist in the proper folding of a variety of cytosolic proteins. GroEL utilizes two metal cofactors, Mg(2+) and K(+), to bind and hydrolyze ATP. A K(+)-binding site has been proposed to be located next to the nucleotide-binding site, but the available structural data do not firmly support this conclusion. Moreover, more than one functionally significant K(+)-binding site may exist within GroEL. Because K(+) has important and complex effects on GroEL activity and is involved in both positive (intra-ring) and negative (inter-ring) cooperativity for ATP hydrolysis, it is important to determine the exact location of these cation-binding site(s) within GroEL. In this study, the K(+) mimetic Tl(+) was incorporated into GroEL crystals, a moderately redundant 3.94 A resolution X-ray diffraction data set was collected from a single crystal and the strong anomalous scattering signal from the thallium ion was used to identify monovalent cation-binding sites. The results confirmed the previously proposed placement of K(+) next to the nucleotide-binding site and also identified additional binding sites that may be important for GroEL function and cooperativity. These findings also demonstrate the general usefulness of Tl(+) for the identification of monovalent cation-binding sites in protein crystal structures, even when the quality and resolution of the diffraction data are relatively low. Use of thallium to identify monovalent cation binding sites in GroEL.,Kiser PD, Lorimer GH, Palczewski K Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Oct 1;65(Pt, 10):967-71. Epub 2009 Sep 18. PMID:19851000 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Chaperonin Heat Shock Proteins

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