1r62
From Proteopedia
(New page: 200px<br /><applet load="1r62" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r62, resolution 1.60Å" /> '''Crystal structure of...) |
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| - | [[Image:1r62.jpg|left|200px]]<br /><applet load="1r62" size=" | + | [[Image:1r62.jpg|left|200px]]<br /><applet load="1r62" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1r62, resolution 1.60Å" /> | caption="1r62, resolution 1.60Å" /> | ||
'''Crystal structure of the C-terminal Domain of the Two-Component System Transmitter Protein NRII (NtrB)'''<br /> | '''Crystal structure of the C-terminal Domain of the Two-Component System Transmitter Protein NRII (NtrB)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The kinase/phosphatase nitrogen regulator II (NRII, NtrB) is a member of | + | The kinase/phosphatase nitrogen regulator II (NRII, NtrB) is a member of the transmitter protein family of conserved two-component signal transduction systems. The kinase activity of NRII brings about the phosphorylation of the transcription factor nitrogen regulator I (NRI, NtrC), causing the activation of Ntr gene transcription. The phosphatase activity of NRII results in the inactivation of NRI-P. The activities of NRII are regulated by the signal transduction protein encoded by glnB, PII protein, which upon binding to NRII inhibits the kinase and activates the phosphatase activity. The C-terminal ATP-binding domain of NRII is required for both the kinase and phosphatase activities and contains the PII binding site. Here, we present the crystal structure of the C-terminal domain of a mutant form of NRII, NRII-Y302N, at 1.6 A resolution and compare this structure to the analogous domains of other two-component system transmitter proteins. While the C-terminal domain of NRII shares the general tertiary structure seen in CheA, PhoQ, and EnvZ transmitter proteins, it contains a distinct beta-hairpin projection that is absent in these related proteins. This projection is near the site of a well-characterized mutation that reduces the binding of PII and near other less-characterized mutations that affect the phosphatase activity of NRII. Sequence alignment suggests that the beta-hairpin projection is present in NRII proteins from various organisms, and absent in other transmitter proteins from Escherichia coliK-12. This unique structural element in the NRII C-terminal domain may play a role in binding PII or in intramolecular signal transduction. |
==About this Structure== | ==About this Structure== | ||
| - | 1R62 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:// | + | 1R62 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=1R62 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Ninfa, A | + | [[Category: Ninfa, A J.]] |
[[Category: Peisach, D.]] | [[Category: Peisach, D.]] | ||
| - | [[Category: Pioszak, A | + | [[Category: Pioszak, A A.]] |
[[Category: Song, Y.]] | [[Category: Song, Y.]] | ||
[[Category: Xu, Z.]] | [[Category: Xu, Z.]] | ||
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[[Category: two component system]] | [[Category: two component system]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:47:28 2008'' |
Revision as of 12:47, 21 February 2008
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Crystal structure of the C-terminal Domain of the Two-Component System Transmitter Protein NRII (NtrB)
Overview
The kinase/phosphatase nitrogen regulator II (NRII, NtrB) is a member of the transmitter protein family of conserved two-component signal transduction systems. The kinase activity of NRII brings about the phosphorylation of the transcription factor nitrogen regulator I (NRI, NtrC), causing the activation of Ntr gene transcription. The phosphatase activity of NRII results in the inactivation of NRI-P. The activities of NRII are regulated by the signal transduction protein encoded by glnB, PII protein, which upon binding to NRII inhibits the kinase and activates the phosphatase activity. The C-terminal ATP-binding domain of NRII is required for both the kinase and phosphatase activities and contains the PII binding site. Here, we present the crystal structure of the C-terminal domain of a mutant form of NRII, NRII-Y302N, at 1.6 A resolution and compare this structure to the analogous domains of other two-component system transmitter proteins. While the C-terminal domain of NRII shares the general tertiary structure seen in CheA, PhoQ, and EnvZ transmitter proteins, it contains a distinct beta-hairpin projection that is absent in these related proteins. This projection is near the site of a well-characterized mutation that reduces the binding of PII and near other less-characterized mutations that affect the phosphatase activity of NRII. Sequence alignment suggests that the beta-hairpin projection is present in NRII proteins from various organisms, and absent in other transmitter proteins from Escherichia coliK-12. This unique structural element in the NRII C-terminal domain may play a role in binding PII or in intramolecular signal transduction.
About this Structure
1R62 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure of the C-terminal domain of the two-component system transmitter protein nitrogen regulator II (NRII; NtrB), regulator of nitrogen assimilation in Escherichia coli., Song Y, Peisach D, Pioszak AA, Xu Z, Ninfa AJ, Biochemistry. 2004 Jun 1;43(21):6670-8. PMID:15157101
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