PXD006008

PXD006008 is an original dataset announced via ProteomeXchange.

Title	Large scale investigation of the phage Vp16 PDF activity
Description	Prokaryotic proteins must be deformylated before the removal of their first methionine. Peptide deformylase (PDF) is indispensable and guarantees this cotranslational mechanism. Recent genome sequencing and annotation studies highlighted over 2x104 putative peptide deformylase sequences. Furthermore, unpredicted modified bacterial PDF genes have been retrieved from many phages. Sequence comparisons with other known PDFs reveal that viral PDFs are devoid of the key ribosome-interacting C-terminal region. Little is known regarding these viral PDFs, including the capacity of the corresponding encoded proteins to ensure deformylase activity in vitro or in vivo. This investigation determines the activity of the recombinant Vp16 PDF in E. coli PDF defective cell to remove the N-formyl group at the protein N-terminus.
HostingRepository	PRIDE
AnnounceDate	2017-09-25
AnnouncementXML	Submission_2017-09-25_02:17:29.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Willy Bienvenut
SpeciesList	scientific name: Escherichia coli; NCBI TaxID: 562;
ModificationList	acetate labeling reagent (N-term) (heavy form: +3amu); alpha-amino acetylated residue; 3x(2)H labeled N6-acetyl-L-lysine; N-formylated residue; monohydroxylated residue; iodoacetamide derivatized residue
Instrument	LTQ Orbitrap Velos

Revision	Datetime	Status	ChangeLog Entry
0	2017-03-03 02:06:57	ID requested
⏵ 1	2017-09-25 02:17:30	announced

Grzela R, Nusbaum J, Fieulaine S, Lavecchia F, Bienvenut WV, Dian C, Meinnel T, Giglione C, The C-terminal residue of phage Vp16 PDF, the smallest peptide deformylase, acts as an offset element locking the active conformation. Sci Rep, 7(1):11041(2017) [pubmed]

curator keyword: Biological

submitter keyword: peptide deformylase, virus, phage, metalloenzyme, N-terminal methionine excision

Willy Vincent Bienvenut
contact affiliation	Institute of Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Bâtiment 23A, 1 avenue de la Terrasse, F-91198 Gif-sur-Yvette cedex, France.
contact email	willy.bienvenut@i2bc.paris-saclay.fr
lab head
Willy Bienvenut
contact affiliation	CNRS
contact email	willy.bienvenut@i2bc.paris-saclay.fr
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2017/09/PXD006008

PRIDE project URI

• PRIDE
  1. PXD006008
     1. Label: PRIDE project
     2. Name: Large scale investigation of the phage Vp16 PDF activity