2jnv
From Proteopedia
(New page: 200px<br /><applet load="2jnv" size="350" color="white" frame="true" align="right" spinBox="true" caption="2jnv" /> '''Solution structure of C-terminal domain of N...) |
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==Overview== | ==Overview== | ||
| - | OsCnfU-1A is a chloroplast-type Nfu-like protein that consists of tandem | + | OsCnfU-1A is a chloroplast-type Nfu-like protein that consists of tandem repeats sharing high sequence homology. Domain I of this protein, but not domain II, has a C-X-X-C motif that is thought to assemble an iron-sulphur cluster. Herein we report the solution structure of OsCnfU-1A domain I (73-153). Although OsCnfU-1A domain I is structurally similar to OsCnfU-1A domain II (154-226), the electrostatic surface potential of the 2 domains differs. Domain I has an acidic surface, whereas that of domain II is predominantly basic. Chemical shift perturbation studies on OsCnfU-1A domain I and domain II with ferredoxin revealed negligible chemical shift changes in domain I, whereas much larger chemical shift changes were observed in domain II. The residues with larger chemical shift changes were located on the basic surface of domain II. Considering that ferredoxin is predominantly negatively charged, we propose the following hypothesis: First, an iron-sulphur cluster is assembled on domain I. Next, domain II interacts with the ferredoxin, thus tethering domain I close to the ferredoxin. Finally, domain I transfers the iron-sulphur cluster to the ferredoxin. Thus, domain II facilitates the efficient transfer of the iron-sulphur cluster from domain I to the ferredoxin. |
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | The cooperative role of OsCnfU-1A domain I and domain II in the iron sulphur cluster transfer process as revealed by NMR., Saio T, Kumeta H, Ogura K, Yokochi M, Asayama M, Katoh S, Katoh E, Teshima K, Inagaki F, J Biochem | + | The cooperative role of OsCnfU-1A domain I and domain II in the iron sulphur cluster transfer process as revealed by NMR., Saio T, Kumeta H, Ogura K, Yokochi M, Asayama M, Katoh S, Katoh E, Teshima K, Inagaki F, J Biochem. 2007 Jul;142(1):113-21. Epub 2007 Jun 1. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17545250 17545250] |
[[Category: Oryza sativa]] | [[Category: Oryza sativa]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Kumeta, H.]] | [[Category: Kumeta, H.]] | ||
[[Category: Ogura, K.]] | [[Category: Ogura, K.]] | ||
| - | [[Category: RSGI, RIKEN | + | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] |
[[Category: Saio, T.]] | [[Category: Saio, T.]] | ||
[[Category: Yokochi, M.]] | [[Category: Yokochi, M.]] | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:04:31 2008'' |
Revision as of 16:04, 21 February 2008
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Solution structure of C-terminal domain of NifU-like protein from Oryza sativa
Overview
OsCnfU-1A is a chloroplast-type Nfu-like protein that consists of tandem repeats sharing high sequence homology. Domain I of this protein, but not domain II, has a C-X-X-C motif that is thought to assemble an iron-sulphur cluster. Herein we report the solution structure of OsCnfU-1A domain I (73-153). Although OsCnfU-1A domain I is structurally similar to OsCnfU-1A domain II (154-226), the electrostatic surface potential of the 2 domains differs. Domain I has an acidic surface, whereas that of domain II is predominantly basic. Chemical shift perturbation studies on OsCnfU-1A domain I and domain II with ferredoxin revealed negligible chemical shift changes in domain I, whereas much larger chemical shift changes were observed in domain II. The residues with larger chemical shift changes were located on the basic surface of domain II. Considering that ferredoxin is predominantly negatively charged, we propose the following hypothesis: First, an iron-sulphur cluster is assembled on domain I. Next, domain II interacts with the ferredoxin, thus tethering domain I close to the ferredoxin. Finally, domain I transfers the iron-sulphur cluster to the ferredoxin. Thus, domain II facilitates the efficient transfer of the iron-sulphur cluster from domain I to the ferredoxin.
About this Structure
2JNV is a Single protein structure of sequence from Oryza sativa. Full crystallographic information is available from OCA.
Reference
The cooperative role of OsCnfU-1A domain I and domain II in the iron sulphur cluster transfer process as revealed by NMR., Saio T, Kumeta H, Ogura K, Yokochi M, Asayama M, Katoh S, Katoh E, Teshima K, Inagaki F, J Biochem. 2007 Jul;142(1):113-21. Epub 2007 Jun 1. PMID:17545250
Page seeded by OCA on Thu Feb 21 18:04:31 2008
Categories: Oryza sativa | Single protein | Inagaki, F. | Katoh, E. | Katoh, S. | Kumeta, H. | Ogura, K. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Saio, T. | Yokochi, M. | Iron-sulfur cluster binding | Metal transport | National project on protein structural and functional analyses | Nppsfa | Program for rice genome reserch | Riken structural genomics/proteomics initiative | Rsgi | Structural genomics
