User:Susana Retamal/Sandbox1: Difference between revisions

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=Background Information=
=Background Information=


Rsp1275 is a member of the Fnr-Crp family of transcriptional regulators. Homologues of the Fnr protein from ''E. coli'' have been identified in a variety of taxonomically diverse bacterial species. <ref>Spiro, S. 1994. The FNR family of transcriptional regulators. Antonie van Leeuwenhoek 66:23–36.</ref>. <ref>PredictProtein: B Rost, G Yachdav and J Liu (2004). The PredictProtein Server. Nucleic Acids Research 32(Web Server issue):W321-W326.</ref>The bacterium ''Rhodobacter sphaeroides 2.4.1'' encodes 8 members of this family, however only 2 have known function. The modeling of 7 of them were successfully obtained using 3D-Jigsaw, all being very similar in structure to Crp (the only one with crystal structure solved). The DNA binding domain helix-turn-helix is located in the C-terminal, and the N-terminal part contains the allosteric effector domain. Rsp1275 has been linked with salt-tolerance in ''Rhodobacter spheroides''. Different genes coding for the Fnr-Crp proteins of unknown function have been cloned and a multicopy test was performed to evaluate these as potential regulators of NaCl-responsive genes.  
Rsp1275 is a member of the Fnr-Crp family of transcriptional regulators. Homologues of the Fnr protein from ''E. coli'' have been identified in a variety of taxonomically diverse bacterial species. <ref>Spiro, S. 1994. The FNR family of transcriptional regulators. Antonie van Leeuwenhoek 66:23–36.</ref><ref>PredictProtein: B Rost, G Yachdav and J Liu (2004). The PredictProtein Server. Nucleic Acids Research 32(Web Server issue):W321-W326.</ref>The bacterium ''Rhodobacter sphaeroides" 2.4.1 encodes 8 members of this family, however only 2 have known function. Models of 7 of them, including RSP1275, were successfully obtained using 3D-Jigsaw, all being very similar in structure to Crp (the only one with crystal structure solved). The DNA binding domain helix-turn-helix is located in the C-terminal, and the N-terminal part contains the allosteric effector domain.  
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= Structure of the Proposed rsp1275 modeling obtained using 3D-Jigsaw =
= Structure of the Proposed rsp1275 modeling obtained using 3D-Jigsaw =
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<applet load='Rsp1275.pdb' size='300' frame='true' align='right' caption='Insert caption here' />
<applet load='Rsp1275.pdb' size='300' frame='true' align='right' caption='Insert caption here' />


The highlighted <scene name='User:Susana_Retamal/Sandbox1/Rsp1275/10'>aplha-helices</scene> of the protein.
The highlighted <scene name='User:Susana_Retamal/Sandbox1/Rsp1275/10'>alpha-helices</scene> of the protein.


This is the <scene name='User:Susana_Retamal/Sandbox1/Rsp1275/12'>Amino to Carboxyl rainbow</scene> of the protein.
This is the <scene name='User:Susana_Retamal/Sandbox1/Rsp1275/12'>Amino to Carboxyl rainbow</scene> of the protein.
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=Evidence of Fnr-Crp protein Involvement in Transcriptional Response to NaCl=
It has been proposed that Fnr-Crp protein encoded by rsp1275 is a transcription factor responsible for salt-responsive changes in the transcriptome. In addition, it's likely that rsp1275 interacts with a small ligand (potentially Na or Cl).


=Physico - Chemical parameters for Rsp1275=  
=Physico - Chemical parameters for Rsp1275=