Summary for 2WQK
| Entry DOI | 10.2210/pdb2wqk/pdb |
| Descriptor | 5'-NUCLEOTIDASE SURE, SULFATE ION, SODIUM ION, ... (4 entities in total) |
| Functional Keywords | sure protein, putative acid phosphatase, structural genomics, 3-d structure, mixed alpha/beta protein, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi, hydrolase |
| Biological source | AQUIFEX AEOLICUS |
| Total number of polymer chains | 2 |
| Total formula weight | 56632.58 |
| Authors | Antonyuk, S.V.,Ellis, M.J.,Strange, R.W.,Hasnain, S.S.,Bessho, Y.,Kuramitsu, S.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2009-08-23, release date: 2009-09-29, Last modification date: 2023-12-20) |
| Primary citation | Antonyuk, S.V.,Ellis, M.J.,Strange, R.W.,Bessho, Y.,Kuramitsu, S.,Shinkai, A.,Yokoyama, S.,Hasnain, S.S. Structure of Sure Protein from Aquifex Aeolicus Vf5 at 1.5 A Resolution. Acta Crystallogr.,Sect.F, 65:1204-, 2009 Cited by PubMed Abstract: SurE is a stationary-phase survival protein found in bacteria, eukaryotes and archaea that exhibits a divalent-metal-ion-dependent phosphatase activity and acts as a nucleotidase and polyphosphate phosphohydrolase. The structure of the SurE protein from the hyperthermophile Aquifex aeolicus has been solved at 1.5 A resolution using molecular replacement with one dimer in the asymmetric unit and refined to an R factor of 15.6%. The crystal packing reveals that two dimers assemble to form a tetramer, although gel-filtration chromatography showed the presence of only a dimer in solution. The phosphatase active-site pocket was occupied by sulfate ions from the crystallization medium. PubMed: 20054112DOI: 10.1107/S1744309109043814 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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