2IY4
X-ray structure of Dps from Listeria monocytogenes
Summary for 2IY4
| Entry DOI | 10.2210/pdb2iy4/pdb |
| Descriptor | NON-HEME IRON-CONTAINING FERRITIN, FE (III) ION (3 entities in total) |
| Functional Keywords | iron, iron storage, metal-binding, oxidative damage, dpslm (dna-binding protein from starved cells) from lister iron-incorporation, metal-binding protein, metal binding protein |
| Biological source | LISTERIA MONOCYTOGENES |
| Cellular location | Cytoplasm (By similarity): Q8Y8G1 |
| Total number of polymer chains | 24 |
| Total formula weight | 434984.66 |
| Authors | Ilari, A.,Bellapadrona, G.,Stefanini, S.,Chiancone, E. (deposition date: 2006-07-12, release date: 2007-01-02, Last modification date: 2023-12-13) |
| Primary citation | Bellapadrona, G.,Chiaraluce, R.,Consalvi, V.,Ilari, A.,Stefanini, S.,Chiancone, E. The Mutations Lys 114 --> Gln and Asp 126 --> Asn Disrupt an Intersubunit Salt Bridge and Convert Listeria Innocua Dps Into its Natural Mutant Listeria Monocytogenes Dps. Effects on Protein Stability at Low Ph. Proteins, 66:975-, 2007 Cited by PubMed Abstract: The stability of the dodecameric Listeria monocytogenes Dps has been compared with that of the Listeria innocua protein. The two proteins differ only in two amino acid residues that form an intersubunit salt-bridge in L. innocua Dps. This salt-bridge is replaced by a hydrogen bonding network in L. monocytogenes Dps as revealed by the X-ray crystal structure. The resistance to low pH and high temperature was assayed for both Dps proteins under equilibrium conditions and kinetically. Despite the identical equilibrium behavior, significant differences in the kinetic stability and activation energy of the unfolding process are apparent at pH 1.5. The higher stability of L. monocytogenes Dps has been accounted for in terms of the persistence of the hydrogen bonding network at this low pH value. In contrast, the salt-bridge between Lys 114 and Asp 126 characteristic of L. innocua Dps is most likely abolished due to protonation of Asp 126. PubMed: 17186524DOI: 10.1002/PROT.21305 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.31 Å) |
Structure validation
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