Nagendra, HG and Sudarsankumar, C and Vijayan, M (1996) An X-ray Analysis of Native Monoclinic Lysozyme. A Case Study on the Reliability of Refined Protein Structures and a Comparison with the Low-Humidity Form in Relation to Mobility and Enzyme Action. In: Acta Crystallographica Section D, 52 . pp. 1067-1074.
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The atomic models of native monoclinic lysozyme obtained by refinement at Bangalore and elsewhere [Young, Dewan, Nave & Tilton (1993). J. Appl. Co'st. 26, 309-319] differed significantly in the flexible regions of the protein molecule. The two models were reconciled starting from regions where they were in reasonable agreement to produce an improved model which yielded an R value of 0.169 for 12 816 observed reflections in the 10-2,~, resolution range. The reconciled model was compared with the structure of the 88 % relative humidity form obtained through water mediated transformation [Madhusudan, Kodandapani & Vijayan (1993). Acta Co, st. D49, 234-245]. Parts of the flexible regions of the molecule register significant movements during the transformation. The changes resulting from the transformation from the native to the low-humidity forms are pronounced in many of the side chains in the active-site region, thus indicating the relationship between hydration, mobility and enzyme action. The fact that the overall changes in molecular geometry resulting from water-mediated transformation are similar to those which occur during enzyme action, further emphasizes this relationship.
|Item Type:||Journal Article|
|Additional Information:||The copyright belongs to International Union of Crystallography|
|Keywords:||x ray analysis;lysozyme;protein structures;enzyme action|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit|
|Date Deposited:||03 Aug 2004|
|Last Modified:||19 Sep 2010 04:14|
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