1ew0
From Proteopedia
(New page: 200px<br /><applet load="1ew0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ew0, resolution 1.4Å" /> '''CRYSTAL STRUCTURE ANA...) |
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| - | [[Image:1ew0.gif|left|200px]]<br /><applet load="1ew0" size=" | + | [[Image:1ew0.gif|left|200px]]<br /><applet load="1ew0" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ew0, resolution 1.4Å" /> | caption="1ew0, resolution 1.4Å" /> | ||
'''CRYSTAL STRUCTURE ANALYSIS OF THE SENSOR DOMAIN OF RMFIXL(FERROUS FORM)'''<br /> | '''CRYSTAL STRUCTURE ANALYSIS OF THE SENSOR DOMAIN OF RMFIXL(FERROUS FORM)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | FixL of Rhizobium meliloti (RmFixL) is a sensor histidine kinase of the | + | FixL of Rhizobium meliloti (RmFixL) is a sensor histidine kinase of the two-component system, which regulates the expression of the genes related to nitrogen fixation in the root nodule in response to the O(2) levels. The crystal structure of the sensor domain of FixL (RmFixLH), which contains a heme (Fe-porphyrin) as a sensing site, was determined at 1.4 A resolution. Based on the structural and spectroscopic analyses, we propose the O(2) sensing mechanism that differs from the case proposed in BjFixLH as follows; conformational changes in the F/G loop, which are induced by steric repulsion between the bent-bound O(2) and the Ile209 side-chain, would be transmitted to the histidine kinase domain. Interaction between the iron-bound O(2) and Ile209 was also observed in the resonance Raman spectra of RmFixLH as evidenced by the fact that the Fe-O(2) and Fe-CN stretching frequencies were shifted from 575 to 570 cm(-1) (Fe-O(2)), and 504 to 499 cm(-1), respectively, as the result of the replacement of Ile209 with an Ala residue. In the I209A mutant of RmFixL, the O(2) sensing activity was destroyed, thus confirming our proposed mechanism. |
==About this Structure== | ==About this Structure== | ||
| - | 1EW0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sinorhizobium_meliloti Sinorhizobium meliloti] with HEM as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1EW0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sinorhizobium_meliloti Sinorhizobium meliloti] with <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EW0 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Nakamura, H.]] | [[Category: Nakamura, H.]] | ||
[[Category: Nakamura, K.]] | [[Category: Nakamura, K.]] | ||
| - | [[Category: Park, S | + | [[Category: Park, S Y.]] |
[[Category: Shiro, Y.]] | [[Category: Shiro, Y.]] | ||
[[Category: Tamura, K.]] | [[Category: Tamura, K.]] | ||
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[[Category: rhizobium meliloti]] | [[Category: rhizobium meliloti]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:32:05 2008'' |
Revision as of 10:32, 21 February 2008
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CRYSTAL STRUCTURE ANALYSIS OF THE SENSOR DOMAIN OF RMFIXL(FERROUS FORM)
Overview
FixL of Rhizobium meliloti (RmFixL) is a sensor histidine kinase of the two-component system, which regulates the expression of the genes related to nitrogen fixation in the root nodule in response to the O(2) levels. The crystal structure of the sensor domain of FixL (RmFixLH), which contains a heme (Fe-porphyrin) as a sensing site, was determined at 1.4 A resolution. Based on the structural and spectroscopic analyses, we propose the O(2) sensing mechanism that differs from the case proposed in BjFixLH as follows; conformational changes in the F/G loop, which are induced by steric repulsion between the bent-bound O(2) and the Ile209 side-chain, would be transmitted to the histidine kinase domain. Interaction between the iron-bound O(2) and Ile209 was also observed in the resonance Raman spectra of RmFixLH as evidenced by the fact that the Fe-O(2) and Fe-CN stretching frequencies were shifted from 575 to 570 cm(-1) (Fe-O(2)), and 504 to 499 cm(-1), respectively, as the result of the replacement of Ile209 with an Ala residue. In the I209A mutant of RmFixL, the O(2) sensing activity was destroyed, thus confirming our proposed mechanism.
About this Structure
1EW0 is a Single protein structure of sequence from Sinorhizobium meliloti with as ligand. Full crystallographic information is available from OCA.
Reference
Sensory mechanism of oxygen sensor FixL from Rhizobium meliloti: crystallographic, mutagenesis and resonance Raman spectroscopic studies., Miyatake H, Mukai M, Park SY, Adachi S, Tamura K, Nakamura H, Nakamura K, Tsuchiya T, Iizuka T, Shiro Y, J Mol Biol. 2000 Aug 11;301(2):415-31. PMID:10926518
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