1z0r

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

spinqualitylabelsall models 1z0r Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1z0r is a 2 chain structure with sequence from Bacillus subtilis. This structure supersedes the now removed PDB entry 1ekt. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ABRB_BACSU Ambiactive repressor and activator of the transcription of genes expressed during the transition state between vegetative growth and the onset of stationary phase and sporulation. It controls the expression of genes spovG and tycA. AbrB binds to the tycA promoter region at two A- and T-rich sites, it may be the sole repressor of tycA transcription. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Revised structure of the AbrB N-terminal domain unifies a diverse superfamily of putative DNA-binding proteins.,Bobay BG, Andreeva A, Mueller GA, Cavanagh J, Murzin AG FEBS Lett. 2005 Oct 24;579(25):5669-74. Epub 2005 Oct 4. PMID:16223496 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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