5l8z

Structure of thermostable DNA-binding HU protein from micoplasma Spiroplasma melliferum

spinqualitylabelsall models 5l8z, resolution 1.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5l8z is a 1 chain structure with sequence from Spiroplasma melliferum KC3. This structure supersedes the now removed PDB entries 4n1v and 5cvx. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.4Å Ligands: NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A037USE5_SPIME Publication Abstract from PubMed The three-dimensional structure of the histone-like HU protein from the mycoplasma Spiroplasma melliferum KC3 (HUSpm) was determined at 1.4 A resolution, and the thermal stability of the protein was evaluated by differential scanning calorimetry. A detailed analysis revealed that the three-dimensional structure of the HUSpm dimer is similar to that of its bacterial homologues but is characterized by stronger hydrophobic interactions at the dimer interface. This HUSpm dimer interface lacks salt bridges but is stabilized by a larger number of hydrogen bonds. According to the DSC data, HUSpm has a high denaturation temperature, comparable to that of HU proteins from thermophilic bacteria. To elucidate the structural basis of HUSpm thermal stability, we identified amino acid residues potentially responsible for this property and modified them by site-directed mutagenesis. A comparative analysis of the melting curves of mutant and wild-type HUSpm revealed the motifs that play a key role in protein thermal stability: non-conserved phenylalanine residues in the hydrophobic core, an additional hydrophobic loop at the N-terminal region of the protein, the absence of the internal cavity present at the dimer interface of some HU proteins, and the presence of additional hydrogen bonds between the monomers that are missing in homologous proteins. Structural basis of the high thermal stability of the histone-like HU protein from the mollicute Spiroplasma melliferum KC3.,Boyko KM, Rakitina TV, Korzhenevskiy DA, Vlaskina AV, Agapova YK, Kamashev DE, Kleymenov SY, Popov VO Sci Rep. 2016 Nov 3;6:36366. doi: 10.1038/srep36366. PMID:27808161 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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