2X3F
Crystal Structure of the Methicillin-Resistant Staphylococcus aureus Sar2676, a Pantothenate Synthetase.
Summary for 2X3F
| Entry DOI | 10.2210/pdb2x3f/pdb |
| Descriptor | PANTHOTHENATE SYNTHETASE, DIPHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | ligase, atp-binding, nucleotide-binding, pantothenate biosynthesis |
| Biological source | STAPHYLOCOCCUS AUREUS SUBSP. AUREUS |
| Cellular location | Cytoplasm (Potential): Q6GDK5 |
| Total number of polymer chains | 2 |
| Total formula weight | 64274.69 |
| Authors | Oke, M.,Carter, L.G.,Johnson, K.A.,Liu, H.,Mcmahon, S.A.,White, M.F.,Naismith, J.H. (deposition date: 2010-01-24, release date: 2010-07-21, Last modification date: 2023-12-20) |
| Primary citation | Oke, M.,Carter, L.G.,Johnson, K.A.,Liu, H.,Mcmahon, S.A.,Yan, X.,Kerou, M.,Weikart, N.D.,Kadi, N.,Sheikh, M.A.,Schmelz, S.,Dorward, M.,Zawadzki, M.,Cozens, C.,Falconer, H.,Powers, H.,Overton, I.M.,Van Niekerk, C.A.J.,Peng, X.,Patel, P.,Garrett, R.A.,Prangishvili, D.,Botting, C.H.,Coote, P.J.,Dryden, D.T.F.,Barton, G.J.,Schwarz-Linek, U.,Challis, G.L.,Taylor, G.L.,White, M.F.,Naismith, J.H. The Scottish Structural Proteomics Facility: Targets, Methods and Outputs. J.Struct.Funct.Genom., 11:167-, 2010 Cited by PubMed Abstract: The Scottish Structural Proteomics Facility was funded to develop a laboratory scale approach to high throughput structure determination. The effort was successful in that over 40 structures were determined. These structures and the methods harnessed to obtain them are reported here. This report reflects on the value of automation but also on the continued requirement for a high degree of scientific and technical expertise. The efficiency of the process poses challenges to the current paradigm of structural analysis and publication. In the 5 year period we published ten peer-reviewed papers reporting structural data arising from the pipeline. Nevertheless, the number of structures solved exceeded our ability to analyse and publish each new finding. By reporting the experimental details and depositing the structures we hope to maximize the impact of the project by allowing others to follow up the relevant biology. PubMed: 20419351DOI: 10.1007/S10969-010-9090-Y PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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