1tlv
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1tlv.gif|left|200px]] | [[Image:1tlv.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1tlv", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | + | {{STRUCTURE_1tlv| PDB=1tlv | SCENE= }} | |
| - | + | ||
| - | | | + | |
| - | }} | + | |
'''Structure of the native and inactive LicT PRD from B. subtilis''' | '''Structure of the native and inactive LicT PRD from B. subtilis''' | ||
| Line 31: | Line 28: | ||
[[Category: Tilbeurgh, H van.]] | [[Category: Tilbeurgh, H van.]] | ||
[[Category: Zhou, C Z.]] | [[Category: Zhou, C Z.]] | ||
| - | [[Category: | + | [[Category: Activation mechanism]] |
| - | [[Category: | + | [[Category: Conformational change]] |
| - | [[Category: | + | [[Category: Crystal structure]] |
| - | [[Category: | + | [[Category: Dimer structure]] |
| - | [[Category: | + | [[Category: Histidine phosphorylation]] |
| - | [[Category: | + | [[Category: Hpr]] |
| - | [[Category: | + | [[Category: Lict]] |
| - | [[Category: | + | [[Category: Transcriptional antitermination]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:06:33 2008'' | |
| - | + | ||
| - | + | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 07:06, 3 May 2008
Structure of the native and inactive LicT PRD from B. subtilis
Overview
The transcriptional antiterminator protein LicT regulates the expression of Bacillus subtilis operons involved in beta-glucoside metabolism. It consists of an N-terminal RNA-binding domain (co-antiterminator (CAT)) and two phosphorylatable phosphotransferase system regulation domains (PRD1 and PRD2). In the activated state, each PRD forms a dimeric unit with the phosphorylation sites totally buried at the dimer interface. Here we present the 1.95 A resolution structure of the inactive LicT PRDs as well as the molecular solution structure of the full-length protein deduced from small angle x-ray scattering. Comparison of native (inactive) and mutant (constitutively active) PRD crystal structures shows massive tertiary and quaternary rearrangements of the entire regulatory domain. In the inactive state, a wide swing movement of PRD2 results in dimer opening and brings the phosphorylation sites to the protein surface. This movement is accompanied by additional structural rearrangements of both the PRD1-PRD1 ' interface and the CAT-PRD1 linker. Small angle x-ray scattering experiments indicate that the amplitude of the PRD2 swing might even be wider in solution than in the crystals. Our results suggest that PRD2 is highly mobile in the native protein, whereas it is locked upon activation by phosphorylation.
About this Structure
1TLV is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
Activation of the LicT transcriptional antiterminator involves a domain swing/lock mechanism provoking massive structural changes., Graille M, Zhou CZ, Receveur-Brechot V, Collinet B, Declerck N, van Tilbeurgh H, J Biol Chem. 2005 Apr 15;280(15):14780-9. Epub 2005 Feb 7. PMID:15699035 Page seeded by OCA on Sat May 3 10:06:33 2008
Categories: Bacillus subtilis | Single protein | Collinet, B. | Declerck, N. | Graille, M. | Receveur-Brechot, V. | Tilbeurgh, H van. | Zhou, C Z. | Activation mechanism | Conformational change | Crystal structure | Dimer structure | Histidine phosphorylation | Hpr | Lict | Transcriptional antitermination
