This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


User:Susana Retamal/Sandbox1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 2: Line 2:
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. 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. 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.
 +
''
 +
= Structure of the Proposed rsp1275 modeling obtained using 3D-Jigsaw =
 +
''
-
=''Structure of the Proposed rsp1275 modeling obtained using 3D-Jigsaw'''=
 
<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' />
-
*Highlighted <scene name='User:Susana_Retamal/Sandbox1/Rsp1275/10'>aplha-helices> of the protein.
+
The highlighted <scene name='User:Susana_Retamal/Sandbox1/Rsp1275/10'>aplha-helices> of the protein.
=Protein Sequence=
=Protein Sequence=

Revision as of 19:36, 1 May 2009

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. 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.

Structure of the Proposed rsp1275 modeling obtained using 3D-Jigsaw

Insert caption here

Drag the structure with the mouse to rotate

The highlighted

Proteopedia Page Contributors and Editors (what is this?)

Susana Retamal, Eran Hodis

Personal tools