2X75
Staphylococcus aureus adenylosuccinate lyase
Summary for 2X75
| Entry DOI | 10.2210/pdb2x75/pdb |
| Descriptor | ADENYLOSUCCINATE LYASE, OXALATE ION, ADENOSINE MONOPHOSPHATE, ... (6 entities in total) |
| Functional Keywords | lyase, purine cycle, purine biosynthesis |
| Biological source | STAPHYLOCOCCUS AUREUS |
| Total number of polymer chains | 1 |
| Total formula weight | 50422.28 |
| Authors | Fyfe, P.K.,Dawson, A.,Hutchison, M.T.,Cameron, S.,Hunter, W.N. (deposition date: 2010-02-23, release date: 2010-03-09, Last modification date: 2023-12-20) |
| Primary citation | Fyfe, P.K.,Dawson, A.,Hutchison, M.T.,Cameron, S.,Hunter, W.N. Structure of Staphylococcus Aureus Adenylosuccinate Lyase (Purb) and Assessment of its Potential as a Target for Structure-Based Inhibitor Discovery. Acta Crystallogr.,Sect.D, 66:881-, 2010 Cited by PubMed Abstract: The medium-resolution structure of adenylosuccinate lyase (PurB) from the bacterial pathogen Staphylococcus aureus in complex with AMP is presented. Oxalate, which is likely to be an artifact of crystallization, has been modelled in the active site and occupies a position close to that where succinate is observed in orthologous structures. PurB catalyzes reactions that support the provision of purines and the control of AMP/fumarate levels. As such, the enzyme is predicted to be essential for the survival of S. aureus and to be a potential therapeutic target. Comparisons of this pathogen PurB with the enzyme from Escherichia coli are presented to allow discussion concerning the enzyme mechanism. Comparisons with human PurB suggest that the close similarity of the active sites would make it difficult to identify species-specific inhibitors for this enzyme. However, there are differences in the way that the subunits are assembled into dimers. The distinct subunit-subunit interfaces may provide a potential area to target by exploiting the observation that creation of the enzyme active site is dependent on oligomerization. PubMed: 20693687DOI: 10.1107/S0907444910020081 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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