PXD015568-2

PXD015568 is an original dataset announced via ProteomeXchange.

Title	Insights on the S-layer Deinoxanthin Binding Complex of Deinococcus radiodurans, a massive protein complex with a porin-like structure and function
Description	In Deinococcus radiodurans the outermost Surface layer is tightly matched with the rest of the cell wall into a compact and integrated structure able to contrast environmental adversities. The fundamental unit of this S-layer is the S-layer Deinoxanthin Binding Complex, which has been reported to bind the carotenoid deinoxanthin, to provide thermostability, and ultraviolet radiation resistance. Here we report the low-resolution structural features of this S-layer complex, which has been isolated retaining minor subunits not reported previously. In the present study the S-layer Deinoxanthin Binding Complex is shown to possess peculiar transport functions, as assessed by electrophysiological assays, and a porin-like structural organization, as observed by single particles analysis. In assays on lipid bilayer membranes, the increase in ion current related to the complex insertion, ranged between 10 and 100 pA, suggesting a very broad distribution of the pore sizes. The analysis of the ion current after a few insertions suggested minimal substates of ~0.3-3 nS and likely reflected the unitary conductance. Further assays, based on the reversal potential under different conditions revealed a rather non-selective channel. Eventually, the functional properties of this system and its porin-like organization provide essential elements for understanding the rationale of permeability in bacterial strains carrying S-layers.
HostingRepository	PRIDE
AnnounceDate	2020-02-18
AnnouncementXML	Submission_2020-02-24_03:05:39.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Joanna Kirkpatrick
SpeciesList	scientific name: Deinococcus radiodurans; NCBI TaxID: 1299;
ModificationList	monohydroxylated residue; acetylated residue; iodoacetamide derivatized residue
Instrument	Orbitrap Fusion Lumos

Revision	Datetime	Status	ChangeLog Entry
0	2019-09-24 07:44:20	ID requested
1	2020-02-18 05:49:20	announced
⏵ 2	2020-02-24 03:05:41	announced	2020-02-24: Updated publication reference for PubMed record(s): 32071085.
3	2024-10-22 04:57:22	announced	2024-10-22: Updated project metadata.

Farci D, Aksoyoglu MA, Farci SF, Bafna JA, Bodrenko I, Ceccarelli M, Kirkpatrick J, Winterhalter M, Kere, ï, che S, Piano D, reveal a massive protein complex with porin-like features. J Biol Chem, 295(13):4224-4236(2020) [pubmed]

curator keyword: Biological

submitter keyword: Deinococcus radiodurans, protein complex, S-layer, porin

Dr Dario Piano
contact affiliation	Department of Plant Physiology, Warsaw University of Life Sciences - SGGW, Nowoursynowska Str. 159, 02776, Warsaw, Poland
contact email	dario_piano@sggw.pl
lab head
Joanna Kirkpatrick
contact affiliation	Leibniz Institute on Aging - FLI
contact email	joanna.kirkpatrick@leibniz-fli.de
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD015568
     1. Label: PRIDE project
     2. Name: Insights on the S-layer Deinoxanthin Binding Complex of Deinococcus radiodurans, a massive protein complex with a porin-like structure and function