3zc8

Crystal Structure of Murraya koenigii Miraculin-Like Protein at 2.2 A resolution at pH 7.0

spinqualitylabelsall models 3zc8, resolution 2.24Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3zc8 is a 1 chain structure with sequence from Murraya koenigii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.24Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function D2YW43_MURKO Publication Abstract from PubMed Murraya koenigii miraculin-like protein (MKMLP) gradually precipitates below pH 7.5. Here, we explore the basis for this aggregation by identifying the aggregation-prone regions via comparative analysis of crystal structures acquired at several pH values. The prediction of aggregation-prone regions showed the presence of four short peptides either in beta sheets or loops on surface of the protein. These peptides were distributed in two patches far apart on the surface. Comparison of crystal structures of MKMLP, determined at 2.2 A resolution in pH 7.0 and 4.6 in the present study and determined at 2.9 A in pH 8.0 in an earlier reported study, reveal subtle conformational differences resulting in gradual exposure of aggregation-prone regions. As the pH is lowered, there are alterations in ionic interactions within the protein interactions of the chain with water molecules and exposure of hydrophobic residues. The analysis of symmetry-related molecular interfaces involving one patch revealed shortening of nonpolar intermolecular contacts as the pH decreased. In particular, a decrease in the intermolecular distance between Trp103 of the aggregation-prone peptide WFITTG (103-108) unique to MLPs was observed. These results demonstrated that aggregation occurs due to the cumulative effect of the changes in interactions in two aggregation-prone defined regions. Proteins 2013. (c) 2013 Wiley Periodicals, Inc. Structural insights into the aggregation behavior of Murraya koenigii miraculin-like protein below pH 7.5.,Selvakumar P, Sharma N, Tomar PP, Kumar P, Sharma AK Proteins. 2013 Oct 30. doi: 10.1002/prot.24461. PMID:24265134 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Trypsin inhibitor 3D structures

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