1r62
From Proteopedia
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'''Crystal structure of the C-terminal Domain of the Two-Component System Transmitter Protein NRII (NtrB)''' | '''Crystal structure of the C-terminal Domain of the Two-Component System Transmitter Protein NRII (NtrB)''' | ||
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[[Category: Song, Y.]] | [[Category: Song, Y.]] | ||
[[Category: Xu, Z.]] | [[Category: Xu, Z.]] | ||
| - | [[Category: | + | [[Category: Histidine kinase]] |
| - | [[Category: | + | [[Category: Nrii]] |
| - | [[Category: | + | [[Category: Pii]] |
| - | [[Category: | + | [[Category: Two component system]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:07:40 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 04:07, 3 May 2008
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 Page seeded by OCA on Sat May 3 07:07:40 2008
