1A4X

PYRR, THE BACILLUS SUBTILIS PYRIMIDINE BIOSYNTHETIC OPERON REPRESSOR, HEXAMERIC FORM

Summary for 1A4X

• Entry DOI: 10.2210/pdb1a4x/pdb
• Descriptor: PYRIMIDINE OPERON REGULATORY PROTEIN PYRR, SULFATE ION (3 entities in total)
• Functional Keywords: transcription regulation, attenuation protein, rna-binding protein, pyrimidine biosynthesis, transferase, prtase, phosphoribosyltransferase, bifunctional enzyme
• Biological source: Bacillus subtilis
• Total number of polymer chains: 2
• Total formula weight: 40772.68

Authors

Tomchick, D.R.,Turner, R.J.,Switzer, R.W.,Smith, J.L. (deposition date: 1998-02-08, release date: 1998-08-05, Last modification date: 2024-05-22)

Primary citation

Tomchick, D.R.,Turner, R.J.,Switzer, R.L.,Smith, J.L.
Adaptation of an enzyme to regulatory function: structure of Bacillus subtilis PyrR, a pyr RNA-binding attenuation protein and uracil phosphoribosyltransferase.
Structure, 6:337-350, 1998

PubMed Abstract: The expression of pyrimidine nucleotide biosynthetic (pyr) genes in Bacillus subtilis is regulated by transcriptional attenuation. The PyrR attenuation protein binds to specific sites in pyr mRNA, allowing the formation of downstream terminator structures. UMP and 5-phosphoribosyl-1-pyrophosphate (PRPP), a nucleotide metabolite, are co-regulators with PyrR. The smallest RNA shown to bind tightly to PyrR is a 28-30 nucleotide stem-loop that contains a purine-rich bulge and a putative-GNRA tetraloop. PyrR is also a uracil phosphoribosyltransferase (UPRTase), although the relationship between enzymatic activity and RNA recognition is unclear, and the UPRTase activity of PyrR is not physiologically significant in B. subtilis. Elucidating the role of PyrR structural motifs in UMP-dependent RNA binding is an important step towards understanding the mechanism of pyr transcriptional attenuation.

PubMed: 9551555
DOI: 10.1016/S0969-2126(98)00036-7

Experimental method

X-RAY DIFFRACTION (2.3 Å)