1PIL: Structure Of The Escherichia Coli Signal Transducing Protein Pii

BACKGROUND: In Gram-negative proteobacteria, the nitrogen level in the cell is reflected by the uridylylation status of a key signal transducing protein, PII. PII modulates the activity of glutamine synthetase (GS) through its interaction with adenylyl transferase and it represses the expression of GS by acting in concert with nitrogen regulatory protein II. RESULTS: The three-dimensional structure of the Escherichia coli PII trimer has been determined at 2.7 A resolution. PII shows a low level of structural similarity to a broad family of alpha/beta proteins and contains a double beta alpha beta motif. The PII trimer contains three beta-sheets, each of which is composed of strands from each of the three monomers. These are surrounded by six alpha-helices. CONCLUSIONS: The structure of PII suggests potential regions of interaction with other proteins and serves as an initial step in understanding its signal transducing role in nitrogen regulation.
PDB ID: 1PILDownload
MMDB ID: 57120
PDB Deposition Date: 1994/8/4
Updated in MMDB: 2012/11
Experimental Method:
x-ray diffraction
Resolution: 2.7  Å
Source Organism:
Similar Structures:
Biological Unit for 1PIL: trimeric; determined by author and by software (PISA,PQS)
Molecular Components in 1PIL
Label Count Molecule
Proteins (3 molecules)
Signal Transducing Protein P2(Gene symbol: glnB)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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