1no1
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1no1.jpg|left|200px]] | [[Image:1no1.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1no1", 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_1no1| PDB=1no1 | SCENE= }} | |
| - | | | + | |
| - | | | + | |
| - | }} | + | |
'''Structure of truncated variant of B.subtilis SPP1 phage G39P helicase loader/inhibitor protein''' | '''Structure of truncated variant of B.subtilis SPP1 phage G39P helicase loader/inhibitor protein''' | ||
| Line 34: | Line 31: | ||
[[Category: Sedelnikova, S E.]] | [[Category: Sedelnikova, S E.]] | ||
[[Category: Waltho, J P.]] | [[Category: Waltho, J P.]] | ||
| - | [[Category: | + | [[Category: Bipartite]] |
| - | [[Category: | + | [[Category: Helical]] |
| - | [[Category: | + | [[Category: Natively unfolded domain]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:45:55 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 23:45, 2 May 2008
Structure of truncated variant of B.subtilis SPP1 phage G39P helicase loader/inhibitor protein
Overview
The Bacillus subtilis SPP1 phage-encoded protein G39P is a loader and inhibitor of the phage G40P replicative helicase involved in the initiation of DNA replication. We have carried out a full x-ray crystallographic and preliminary NMR analysis of G39P and functional studies of the protein, including assays for helicase binding by a number of truncated mutant forms, in an effort to improve our understanding of how it both interacts with the helicase and with the phage replisome organizer, G38P. Our structural analyses reveal that G39P has a completely unexpected bipartite structure comprising a folded N-terminal domain and an essentially unfolded C-terminal domain. Although G39P has been shown to bind its G40P target with a 6:6 stoichiometry, our crystal structure and other biophysical characterization data reveal that the protein probably exists predominantly as a monomer in solution. The G39P protein is proteolytically sensitive, and our binding assays show that the C-terminal domain is essential for helicase interaction and that removal of just the 14 C-terminal residues abolishes interaction with the helicase in vitro. We propose a number of possible scenarios in which the flexibility of the C-terminal domain of G39P and its proteolytic sensitivity may have important roles for the function of G39P in vivo that are consistent with other data on SPP1 phage DNA replication.
About this Structure
1NO1 is a Single protein structure of sequence from Bacillus phage spp1. Full crystallographic information is available from OCA.
Reference
Structural analysis of Bacillus subtilis SPP1 phage helicase loader protein G39P., Bailey S, Sedelnikova SE, Mesa P, Ayora S, Waltho JP, Ashcroft AE, Baron AJ, Alonso JC, Rafferty JB, J Biol Chem. 2003 Apr 25;278(17):15304-12. Epub 2003 Feb 13. PMID:12588876 Page seeded by OCA on Sat May 3 02:45:55 2008
