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1pil
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(New page: 200px<br /><applet load="1pil" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pil, resolution 2.7Å" /> '''STRUCTURE OF THE ESCH...)
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Revision as of 21:43, 20 November 2007
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STRUCTURE OF THE ESCHERICHIA COLI SIGNAL TRANSDUCING PROTEIN PII
Overview
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.
About this Structure
1PIL is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structure of the Escherichia coli signal transducing protein PII., Cheah E, Carr PD, Suffolk PM, Vasudevan SG, Dixon NE, Ollis DL, Structure. 1994 Oct 15;2(10):981-90. PMID:7866749
Page seeded by OCA on Tue Nov 20 23:50:30 2007
