4H4L

Crystal Structure of ternary complex of HutP(HutP-L-His-Zn)

Replaces:  2ZH0

Summary for 4H4L

• Entry DOI: 10.2210/pdb4h4l/pdb
• Descriptor: Hut operon positive regulatory protein, HISTIDINE, ZINC ION, ... (4 entities in total)
• Functional Keywords: hutp, anti-termination, histidine metabolism, transcription, transcription regulation, rna binding protein
• Biological source: Bacillus subtilis
• Total number of polymer chains: 12
• Total formula weight: 197449.49

Authors

Dhakshnamoorthy, B.,Misono, T.S.,Mizuno, H.,Kumar, P.K.R. (deposition date: 2012-09-17, release date: 2013-09-04, Last modification date: 2023-11-08)

Primary citation

Dhakshnamoorthy, B.,Mizuno, H.,Kumar, P.K.R.
Alternative binding modes of l-histidine guided by metal ions for the activation of the antiterminator protein HutP of Bacillus subtilis.
J.Struct.Biol., 183:512-518, 2013

PubMed Abstract: Anti-terminator proteins control gene expression by recognizing control signals within cognate transcripts and then preventing transcription termination. HutP is such a regulatory protein that regulates the expression of the histidine utilization (hut) operon in Bacillus subtilis by binding to cis-acting regulatory sequences in hut mRNAs. During the anti-termination process, l-histidine and a divalent ion are required for hutP to bind to the specific sequence within the hut mRNA. Our previous crystal structure of the HutP-l-histidine-Mg(2+)-RNA ternary complex demonstrated that the l-histidine ligand and Mg(2+) bind together such that the backbone nitrogen and carboxyl oxygen of l-histidine coordinate with Mg(2+). In addition to the Mg(2+), other divalent ions are also known to efficiently support the l-histidine-dependent anti-termination of the hut operon, and the best divalent ion is Zn(2+). In this study, we determined the crystal structure of the HutP-l-histidine-Zn(2+) complex and found that the orientation of l-histidine coordinated to Zn(2+) is reversed relative to that of l-histidine coordinated to Mg(2+), i.e., the imidazole side chain nitrogen of l-histidine coordinates to Zn(2+). This alternative binding mode of the l-histidine ligand to a divalent ion provides further insight into the mechanisms responsible for the activation of RNA binding during the hut anti-termination process.

PubMed: 23748184
DOI: 10.1016/j.jsb.2013.05.019

Experimental method

X-RAY DIFFRACTION (2.5 Å)