1cnr | pdb_00001cnr

CORRELATED DISORDER OF THE PURE PRO22(SLASH)LEU25 FORM OF CRAMBIN AT 150K REFINED TO 1.05 ANGSTROMS RESOLUTION

spinqualitylabelsall models 1cnr, resolution 1.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1cnr is a 1 chain structure with sequence from Crambe hispanica subsp. abyssinica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.05Å Ligands: EOH Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CRAM_CRAAB The function of this hydrophobic plant seed protein is not known. 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 The high resolution crystal structure of crambin has been based on the crystals containing two sequence forms (the mixed form). Here, we report the crystal structure of the sequence isomer having Pro and Leu at residues 22 and 25 (the PL form). This elimination of the sequence heterogeneity resulted in a simpler structure which permits a more accurate modeling of protein disorder. In the observed disorder, the PL form structure and the mixed form structure have significant differences: 1) the disorder caused by the sequence heterogeneity (Pro2/Ser22, Leu/Ile25, Tyr29) is absent in the PL form; 2) Phe13 and Glu23 disordered in the mixed form have only one conformation in the PL form; and 3) Asn12 has multiple conformations in the PL form. During the study of disorder in the PL form structure, we found that conformational correlation can be inferred from a structure determined with Bragg's reflections by introducing fundamental stereochemical information, van der Waals contact (Gursky, O., Badger, J., Li, Y., and Caspar, D. L. D. (1992) Biophys. J. 63, 1210-1220), although an x-ray structure is an image averaged over a large number of copies and the period of data collection and does not carry direct evidence about correlations. The correlations among Thr2,Arg10, and Ile34 present the clearest example. The dimension of this correlation is comparable with the short-range (4-8 A) correlations in the atomic displacements concluded from the x-ray diffuse scattering experiments (Caspar, D. L. D., Clarage, J. B., Salunke, D. M., and Clarage, M. S. (1988) Nature 322, 659-662; Clarage, J. B., Clarage, M. S., Phillips, W. C., Sweet, R. M., and Caspar, D. L. D. (1992) Proteins 12, 145-157). Correlated disorder of the pure Pro22/Leu25 form of crambin at 150 K refined to 1.05-A resolution.,Yamano A, Teeter MM J Biol Chem. 1994 May 13;269(19):13956-65. PMID:8188676 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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