1YY7

Crystal structure of stringent starvation protein A (SspA), an RNA polymerase-associated transcription factor

1YY7 の概要

• エントリーDOI: 10.2210/pdb1yy7/pdb
• 分子名称: stringent starvation protein A, CITRIC ACID (3 entities in total)
• 機能のキーワード: gst fold, transcription
• 由来する生物種: Yersinia pestis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 49490.66

構造登録者

Hansen, A.-M.,Gu, Y.,Li, M.,Andrykovitch, M.,Waugh, D.S.,Jin, D.J.,Ji, X. (登録日: 2005-02-23, 公開日: 2005-03-01, 最終更新日: 2023-08-30)

主引用文献

Hansen, A.-M.,Gu, Y.,Li, M.,Andrykovitch, M.,Waugh, D.S.,Jin, D.J.,Ji, X.
Structural basis for the function of stringent starvation protein A as a transcription factor
J.Biol.Chem., 280:17380-17391, 2005

PubMed Abstract: Stringent starvation protein A (SspA) of Escherichia coli is an RNA polymerase-associated transcriptional activator for the lytic development of phage P1 and is essential for stationary phase-induced acid tolerance of E. coli. We report the crystal structure of Yersinia pestis SspA, which is 83% identical to E. coli SspA in amino acid sequence and is functionally complementary in supporting the lytic growth of phage P1 and acid resistance of an E. coli sspA mutant. The structure reveals that SspA assumes the characteristic fold of glutathione S-transferase (GST). However, SspA lacks GST activity and does not bind glutathione. Three regions of SspA are flexible, the N and C termini and the alpha2-helix. The structure also reveals a conserved surface-exposed pocket composed of residues from a loop between helices alpha3 and alpha4. The functional roles of these structural features were investigated by assessing the ability of deletion and site-directed mutants to confer acid resistance of E. coli and to activate transcription from a phage P1 late promoter, thereby supporting the lytic growth of phage P1. The results indicate that the flexible regions are not critical for SspA function, whereas the surface pocket is important for both transcriptional activation of the phage P1 late promoter and acid resistance of E. coli. The size, shape, and property of the pocket suggest that it mediates protein-protein interactions. SspA orthologs from Y. pestis, Vibrio cholerae, and Pseudomonas aeruginosa are all functional in acid resistance of E. coli, whereas only Y. pestis SspA supports phage P1 growth.

PubMed: 15735307
DOI: 10.1074/jbc.M501444200

実験手法

X-RAY DIFFRACTION (2.02 Å)