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Original scientific paper

https://doi.org/10.5562/cca2872

Can Crystal Symmetry and Packing Influence the Active Site Conformation of Homohexameric Purine Nucleoside Phosphorylases?

Marija Luić ; Division of Physical Chemistry, Ruđer Bošković Institute, POB 180, HR-10002 Zagreb, Croatia
Zoran Štefanić ; Division of Physical Chemistry, Ruđer Bošković Institute, POB 180, HR-10002 Zagreb, Croatia


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Abstract

It is generaly believed that enzymes retain most of their functionality in the crystal form due to the large solvent content of protein crystals. This is facilitated by the fact that their natural environment in solution is not too far from the one found in the crystal form. Nevertheless, if the nature of the enzyme is such to require conformational changes, overcoming of the crystal packing constraints may prove to be too difficult. Such conformational change is present in one class of enzymes (purine nucleoside phosphorylases), that is the subject of our scientific interest for many years. The influence of crystal symmetry and crystal packing on the conformation of the active sites in the case of homohexameric purine nucleoside phosphorylases is presented and analysed.

This work is licensed under a Creative Commons Attribution 4.0 International License.

Keywords

crystal symmetry; crystal packing; active site conformation; enzyme reaction; purine nucleoside phosphorylase

Hrčak ID:

166742

URI

https://hrcak.srce.hr/166742

Publication date:

21.6.2016.

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