3W1O

Neisseria DNA mimic protein DMP12

Summary for 3W1O

• Entry DOI: 10.2210/pdb3w1o/pdb
• Descriptor: DNA mimic protein DMP12, MAGNESIUM ION (3 entities in total)
• Functional Keywords: dna mimic, hu protein, protein binding
• Biological source: Neisseria meningitidis MC58
• Total number of polymer chains: 2
• Total formula weight: 28194.38

Authors

Wang, H.C.,Ko, T.P.,Wu, M.L.,Wang, A.H.J. (deposition date: 2012-11-19, release date: 2013-04-10, Last modification date: 2024-03-20)

Primary citation

Wang, H.C.,Wu, M.L.,Ko, T.P.,Wang, A.H.
Neisseria conserved hypothetical protein DMP12 is a DNA mimic that binds to histone-like HU protein
Nucleic Acids Res., 41:5127-5138, 2013

PubMed Abstract: DNA mimic proteins are unique factors that control the DNA-binding activity of target proteins by directly occupying their DNA-binding sites. To date, only a few DNA mimic proteins have been reported and their functions analyzed. Here, we present evidence that the Neisseria conserved hypothetical protein DMP12 should be added to this list. Our gel filtration and analytical ultracentrifugation results showed that the DMP12 monomer interacts with the dimeric form of the bacterial histone-like protein HU. Subsequent structural analysis of DMP12 showed that the shape and electrostatic surface of the DMP12 monomer are similar to those of the straight portion of the bent HU-bound DNA and complementary to those of HU protein dimer. DMP12 also protects HU protein from limited digestion by trypsin and enhances the growth rate Escherichia coli. Functionally, HU proteins participate in bacterial nucleoid formation, as well as recombination, gene regulation and DNA replication. The interaction between DMP12 and HU protein might, therefore, play important roles in these DNA-related mechanisms.

PubMed: 23531546
DOI: 10.1093/nar/gkt201

Experimental method

X-RAY DIFFRACTION (1.85 Å)