1Z0R

Solution Structure of the N-terminal DNA Recognition Domain of the Bacillus subtilis Transcription-State Regulator AbrB

Replaces:  1EKT

Summary for 1Z0R

• Entry DOI: 10.2210/pdb1z0r/pdb
• Related: 1MVF 1N0F
• NMR Information: BMRB: 4281
• Descriptor: Transition state regulatory protein abrB (1 entity in total)
• Functional Keywords: scop database, n-terminal dna-binding domain, transition state regulator, transcription
• Biological source: Bacillus subtilis
• Total number of polymer chains: 2
• Total formula weight: 12222.57

Authors

Bobay, B.G.,Andreeva, A.,Mueller, G.A.,Cavanagh, J.,Murzin, A.G. (deposition date: 2005-03-02, release date: 2005-03-15, Last modification date: 2024-05-29)

Primary citation

Bobay, B.G.,Andreeva, A.,Mueller, G.A.,Cavanagh, J.,Murzin, A.G.
Revised structure of the AbrB N-terminal domain unifies a diverse superfamily of putative DNA-binding proteins.
Febs Lett., 579:5669-5674, 2005

PubMed Abstract: New relationships found in the process of updating the structural classification of proteins (SCOP) database resulted in the revision of the structure of the N-terminal, DNA-binding domain of the transition state regulator AbrB. The dimeric AbrB domain shares a common fold with the addiction antidote MazE and the subunit of uncharacterized protein MraZ implicated in cell division and cell envelope formation. It has a detectable sequence similarity to both MazE and MraZ thus providing an evolutionary link between the two proteins. The putative DNA-binding site of AbrB is found on the same face as the DNA-binding site of MazE and appears similar, both in structure and sequence, to the exposed conserved region of MraZ. This strongly suggests that MraZ also binds DNA and allows for a consensus model of DNA recognition by the members of this novel protein superfamily.

PubMed: 16223496
DOI: 10.1016/j.febslet.2005.09.045

Experimental method

SOLUTION NMR