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2Z90

Crystal Structure of the Second Dps from Mycobacterium smegmatis

Summary for 2Z90
Entry DOI10.2210/pdb2z90/pdb
DescriptorStarvation-inducible DNA-binding protein or fine tangled pili major subunit, FE (II) ION, MAGNESIUM ION, ... (5 entities in total)
Functional Keywordsdna-binding protein, quarternary assembly, ferroxidation, dna binding protein
Biological sourceMycobacterium smegmatis str. MC2 155
Total number of polymer chains4
Total formula weight71762.35
Authors
Roy, S.,Saraswathi, R.,Chatterji, D.,Vijayan, M. (deposition date: 2007-09-13, release date: 2008-04-22, Last modification date: 2023-11-01)
Primary citationRoy, S.,Saraswathi, R.,Chatterji, D.,Vijayan, M.
Structural studies on the second Mycobacterium smegmatis Dps: invariant and variable features of structure, assembly and function.
J.Mol.Biol., 375:948-959, 2008
Cited by
PubMed Abstract: A second DNA binding protein from stationary-phase cells of Mycobacterium smegmatis (MsDps2) has been identified from the bacterial genome. It was cloned, expressed and characterised and its crystal structure was determined. The core dodecameric structure of MsDps2 is the same as that of the Dps from the organism described earlier (MsDps1). However, MsDps2 possesses a long N-terminal tail instead of the C-terminal tail in MsDps1. This tail appears to be involved in DNA binding. It is also intimately involved in stabilizing the dodecamer. Partly on account of this factor, MsDps2 assembles straightway into the dodecamer, while MsDps1 does so on incubation after going through an intermediate trimeric stage. The ferroxidation centre is similar in the two proteins, while the pores leading to it exhibit some difference. The mode of sequestration of DNA in the crystalline array of molecules, as evidenced by the crystal structures, appears to be different in MsDps1 and MsDps2, highlighting the variability in the mode of Dps-DNA complexation. A sequence search led to the identification of 300 Dps molecules in bacteria with known genome sequences. Fifty bacteria contain two or more types of Dps molecules each, while 195 contain only one type. Some bacteria, notably some pathogenic ones, do not contain Dps. A sequence signature for Dps could also be derived from the analysis.
PubMed: 18061613
DOI: 10.1016/j.jmb.2007.10.023
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.4 Å)
Structure validation

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