6NLR
Crystal structure of the putative histidinol phosphatase hisK from Listeria monocytogenes with trinuclear metals determined by PIXE revealing sulphate ion in active site. Based on PIXE analysis and original date from 3DCP
Summary for 6NLR
| Entry DOI | 10.2210/pdb6nlr/pdb |
| Descriptor | Histidinol-phosphatase, MANGANESE (II) ION, COBALT (II) ION, ... (7 entities in total) |
| Functional Keywords | histidinol phosphatase, hisk, histidine biosynthesis, nesg, lmr14, pixe, trinuclear, sulphate, hydrolase |
| Biological source | Listeria monocytogenes serotype 4b str. H7858 |
| Total number of polymer chains | 3 |
| Total formula weight | 99420.13 |
| Authors | Snell, E.H.,Garman, E.F.,Lowe, E.D. (deposition date: 2019-01-09, release date: 2019-12-25, Last modification date: 2024-10-23) |
| Primary citation | Grime, G.W.,Zeldin, O.B.,Snell, M.E.,Lowe, E.D.,Hunt, J.F.,Montelione, G.T.,Tong, L.,Snell, E.H.,Garman, E.F. High-Throughput PIXE as an Essential Quantitative Assay for Accurate Metalloprotein Structural Analysis: Development and Application. J.Am.Chem.Soc., 142:185-197, 2020 Cited by PubMed Abstract: Metalloproteins comprise over one-third of proteins, with approximately half of all enzymes requiring metal to function. Accurate identification of these metal atoms and their environment is a prerequisite to understanding biological mechanism. Using ion beam analysis through particle induced X-ray emission (PIXE), we have quantitatively identified the metal atoms in 30 previously structurally characterized proteins using minimal sample volume and a high-throughput approach. Over half of these metals had been misidentified in the deposited structural models. Some of the PIXE detected metals not seen in the models were explainable as artifacts from promiscuous crystallization reagents. For others, using the correct metal improved the structural models. For multinuclear sites, anomalous diffraction signals enabled the positioning of the correct metals to reveal previously obscured biological information. PIXE is insensitive to the chemical environment, but coupled with experimental diffraction data deposited alongside the structural model it enables validation and potential remediation of metalloprotein models, improving structural and, more importantly, mechanistic knowledge. PubMed: 31794207DOI: 10.1021/jacs.9b09186 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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