Crystallographic analysis of the three-dimensional structure of baboon alpha-lactalbumin at low resolution. Homology with lysozyme
| Autor: | R. Aschaffenburg, S G Smith, R.E. Fenna, M Lewis, David I. Stuart, David Phillips, Ian A. Wilson, M Sundaralingam |
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| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
Models
Molecular Protein Conformation Stereochemistry Crystal structure Biology Biochemistry chemistry.chemical_compound Protein structure X-Ray Diffraction Animals Amino Acid Sequence Molecular Biology Lactalbumin Protein primary structure Cell Biology Protein superfamily Crystallography chemistry X-ray crystallography Alpha-lactalbumin biology.protein Muramidase Lysozyme Research Article Papio |
| Popis: | The crystal structure of baboon alpha-lactalbumin has been determined at 6 A and at 4.5 A (0.6 nm and 0.45 nm) resolution by the method of isomorphous replacement. The principal derivative was prepared by reducing a disulphide bridge in the crystals and inserting a mercury atom. Detailed comparison of the electron-density maps with corresponding maps of hen egg-white lysozyme shows that they are closely similar, with correlation coefficients of 0.57 and 0.44 at 6 A and 4.5 A resolution respectively. This result, in accordance with earlier predictions based upon comparisons of amino-acid sequences, provides further evidence that class C lysozymes and alpha-lactalbumins are homologous proteins and it is in keeping with the hypothesis that the alpha-lactalbumins evolved from a lysozyme precursor. |
| Databáze: | OpenAIRE |
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