1A4X

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

1A4X の概要

• エントリーDOI: 10.2210/pdb1a4x/pdb
• 分子名称: PYRIMIDINE OPERON REGULATORY PROTEIN PYRR, SULFATE ION (3 entities in total)
• 機能のキーワード: transcription regulation, attenuation protein, rna-binding protein, pyrimidine biosynthesis, transferase, prtase, phosphoribosyltransferase, bifunctional enzyme
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 40772.68

構造登録者

Tomchick, D.R.,Turner, R.J.,Switzer, R.W.,Smith, J.L. (登録日: 1998-02-08, 公開日: 1998-08-05, 最終更新日: 2024-05-22)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.3 Å)