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1LQ1

DNA Complexed Structure of the Key Transcription Factor Initiating Development in Sporulation Bacteria

Summary for 1LQ1
Entry DOI10.2210/pdb1lq1/pdb
Descriptor5'-D(*TP*TP*CP*GP*TP*GP*TP*CP*GP*AP*AP*TP*TP*TP*TP*G)-3', 5'-D(*AP*CP*AP*AP*AP*AP*TP*TP*CP*GP*AP*CP*AP*CP*GP*A)-3', Stage 0 sporulation protein A, ... (4 entities in total)
Functional Keywordsspo0a, transcriptional activation and repression, 0a box, dna complexed structure, transcription-dna complex, transcription/dna
Biological sourceBacillus subtilis
Cellular locationCytoplasm (Probable): P06534
Total number of polymer chains8
Total formula weight73178.95
Authors
Zhao, H.,Msadek, T.,Zapf, J.,Madhusudan,Hoch, J.A.,Varughese, K.I. (deposition date: 2002-05-08, release date: 2002-08-23, Last modification date: 2024-02-14)
Primary citationZhao, H.,Msadek, T.,Zapf, J.,Madhusudan,Hoch, J.A.,Varughese, K.I.
DNA complexed structure of the key transcription factor initiating development in sporulating bacteria.
Structure, 10:1041-1050, 2002
Cited by
PubMed Abstract: Sporulation in Bacillus species, the ultimate bacterial adaptive response, requires the precisely coordinated expression of a complex genetic pathway, and is initiated through the accumulation of the phosphorylated form of Spo0A, a pleiotropic response regulator transcription factor. Spo0A controls the transcription of several hundred genes in all spore-forming Bacilli including genes for sporulation and toxin regulation in pathogens such as Bacillus anthracis. The crystal structure of the effector domain of Spo0A from Bacillus subtilis in complex with its DNA target was determined. In the crystal lattice, two molecules form a tandem dimer upon binding to adjacent sites on DNA. The protein:protein and protein:DNA interfaces revealed in the crystal provide a basis for interpreting the transcription activation process and for the design of drugs to counter infections by these bacteria.
PubMed: 12176382
DOI: 10.1016/S0969-2126(02)00803-1
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

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