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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 2.7&Aring;" /> '''STRUCTURE OF THE ESCH...)
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'''STRUCTURE OF THE ESCHERICHIA COLI SIGNAL TRANSDUCING PROTEIN PII'''<br />
'''STRUCTURE OF THE ESCHERICHIA COLI SIGNAL TRANSDUCING PROTEIN PII'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1PIL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PIL OCA].
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1PIL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PIL OCA].
==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Carr, P.D.]]
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[[Category: Carr, P D.]]
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[[Category: Cheah, U.E.]]
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[[Category: Cheah, U E.]]
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[[Category: Ollis, D.L.]]
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[[Category: Ollis, D L.]]
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[[Category: Suffolk, P.M.]]
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[[Category: Suffolk, P M.]]
[[Category: nitrogen regulatory protein]]
[[Category: nitrogen regulatory protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:50:30 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:29:07 2008''

Revision as of 12:29, 21 February 2008

Image:1pil.gif

1pil, resolution 2.7Å

Drag the structure with the mouse to rotate

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

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