NDLI: Structural Analysis of Bacillus subtilis SPP1 Phage Helicase Loader Protein G39P

Content Provider	Journal of Biological Chemistry (JBC)
Author	Bailey, Scott Sedelnikova, Svetlana E. Mesa, Pablo Ayora, Sylvia Waltho, Jon P. Ashcroft, Alison E. Baron, Andrew J. Alonso, Juan C. Rafferty, John B.
Abstract	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.
Related Links	http://www.jbc.org/content/278/17/15304.abstract
Ending Page	15312
Starting Page	15304
Page Count	9
File Format	HTM / HTML PDF
ISSN	00219258
Journal	Journal of Biological Chemistry (JBC)
Issue Number	17
Volume Number	278
DOI	10.1074/jbc.M209300200
e-ISSN	1083351X
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	2003-04-25
Access Restriction	Open
Subject Keyword	GeneX product (GXP) Asymmetric unit (a.u.) Single-stranded (ss) Wild type (wt) 2-[bis(2-hydroxyethyl)amino]-2-(hydroxymethyl)propane-1,3-diol (BisTris) Nickel-nitrilotriacetic acid (Ni-NTA) Adenosine 5′-O-(thiotriphosphate) (ATPγS) PROTEIN STRUCTURE AND FOLDING
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

DNA Structure-specific Nuclease Activities in theSaccharomyces cerevisiae Rad50·Mre11 Complex

A Multisubunit Complex of Outer and Inner Mitochondrial Membrane Protein Translocases Stabilized in Vivo by Translocation Intermediates

Alternative Structural State of Transferrin THE CRYSTALLOGRAPHIC ANALYSIS OF IRON-LOADED BUT DOMAIN-OPENED OVOTRANSFERRIN N-LOBE

Human 75-kDa DNA-pairing Protein Is Identical to the Pro-oncoprotein TLS/FUS and Is Able to Promote D-loop Formation

Pb(II)-translocating P-type ATPases

The Role of Histidines in the Acetate Kinase fromMethanosarcina thermophila

Controlling Polymerization of β-Amyloid and Prion-derived Peptides with Synthetic Small Molecule Ligands

Spectroscopically and Kinetically Distinct Conformational Populations of Sol-Gel-encapsulated Carbonmonoxy Myoglobin A COMPARISON WITH HEMOGLOBIN

Reversibility of Scrapie-associated Prion Protein Aggregation

Structural Analysis of Bacillus subtilis SPP1 Phage Helicase Loader Protein G39P

Similar Documents

DNA Structure-specific Nuclease Activities in theSaccharomyces cerevisiae Rad50·Mre11 Complex

A Multisubunit Complex of Outer and Inner Mitochondrial Membrane Protein Translocases Stabilized in Vivo by Translocation Intermediates

Alternative Structural State of Transferrin THE CRYSTALLOGRAPHIC ANALYSIS OF IRON-LOADED BUT DOMAIN-OPENED OVOTRANSFERRIN N-LOBE

Human 75-kDa DNA-pairing Protein Is Identical to the Pro-oncoprotein TLS/FUS and Is Able to Promote D-loop Formation

Pb(II)-translocating P-type ATPases

The Role of Histidines in the Acetate Kinase fromMethanosarcina thermophila

Controlling Polymerization of β-Amyloid and Prion-derived Peptides with Synthetic Small Molecule Ligands

Spectroscopically and Kinetically Distinct Conformational Populations of Sol-Gel-encapsulated Carbonmonoxy Myoglobin A COMPARISON WITH HEMOGLOBIN

Reversibility of Scrapie-associated Prion Protein Aggregation

Structural Analysis of Bacillus subtilis SPP1 Phage Helicase Loader Protein G39P