About: Engineered Protein Model of the ATP synthase H(+)- Channel Shows No Salt Bridge at the Rotor-Stator Interface

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About: Engineered Protein Model of the ATP synthase H(+)- Channel Shows No Salt Bridge at the Rotor-Stator Interface Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Engineered Protein Model of the ATP synthase H(+)- Channel Shows No Salt Bridge at the Rotor-Stator Interface
Creator	Dmitriev, Oleg Kaler, Mandeep O'grady, Christopher Pierson, Hannah Uhlemann, Eva-Maria
source	Medline; PMC
abstract	ATP synthase is powered by the flow of protons through the molecular turbine composed of two α-helical integral membrane proteins, subunit a, which makes a stator, and a cylindrical rotor assembly made of multiple copies of subunit c. Transient protonation of a universally conserved carboxylate on subunit c (D61 in E. coli) gated by the electrostatic interaction with arginine on subunit a (R210 in E. coli) is believed to be a crucial step in proton transfer across the membrane. We used a fusion protein consisting of subunit a and the adjacent helices of subunit c to test by NMR spectroscopy if cD61 and aR210 are involved in an electrostatic interaction with each other, and found no evidence of such interaction. We have also determined that R140 does not form a salt bridge with either D44 or D124 as was suggested previously by mutation analysis. Our results demonstrate the potential of using arginines as NMR reporter groups for structural and functional studies of challenging membrane proteins.
has issue date	2018-07-27(xsd:dateTime)
bibo:doi	10.1038/s41598-018-29693-z
bibo:pmid	30054535
has license	cc-by
sha1sum (hex)	69360aaa87b55456c581620207955ad5fe24223b
schema:url	https://doi.org/10.1038/s41598-018-29693-z
resource representing a document's title	Engineered Protein Model of the ATP synthase H(+)- Channel Shows No Salt Bridge at the Rotor-Stator Interface
has PubMed Central identifier	PMC6063947
has PubMed identifier	30054535
schema:publication	Sci Rep
resource representing a document's body	covid:69360aaa87b55456c581620207955ad5fe24223b#body_text
is schema:about of	named entity 'fusion protein' named entity 'powered' named entity 'structural' named entity 'electrostatic interaction' named entity 'cD61' named entity 'mutation analysis' named entity 'stator' named entity 'Transient' named entity 'Channel' named entity 'PREVIOUSLY' named entity 'ROTOR' named entity 'MULTIPLE' named entity 'GATED' named entity 'ELECTROSTATIC INTERACTION' named entity 'OPEN' named entity 'CHANNEL' named entity 'ASSEMBLY' named entity 'PROTEIN ' named entity 'POTENTIAL' named entity 'HELICAL' named entity 'COMPOSED OF' named entity 'SALT BRIDGE' named entity 'OUR' named entity 'INTERACTION' named entity 'STATOR' named entity 'PROTONATION' named entity 'SUBUNIT' named entity 'CONSERVED' named entity 'POWERED' named entity 'PROTONS' named entity 'D44' named entity 'SALT BRIDGE' named entity 'PROTEIN MODEL' named entity 'NO EVIDENCE OF' named entity 'HELICES' named entity 'MEMBRANE' named entity 'INVOLVED' named entity 'MUTATION ANALYSIS' named entity 'DOES NOT' named entity 'MEMBRANE PROTEINS' named entity 'FOUND' named entity 'ACROSS' named entity 'CARBOXYLATE' named entity 'DETERMINED' named entity 'FLOW' named entity 'NMR SPECTROSCOPY' named entity 'TO TEST' named entity 'USING' named entity 'INTEGRAL MEMBRANE PROTEINS' named entity 'STRUCTURAL' named entity 'COPIES' named entity 'USED' named entity 'STEP' named entity 'HAVE' named entity 'EITHER' named entity 'TRANSIENT' named entity 'REPORTER' named entity 'STUDIES' named entity 'ENGINEERED PROTEIN' named entity 'RESULTS' named entity 'E. COLI' named entity 'ARGININE' named entity 'CD61' named entity 'FUSION PROTEIN' named entity 'GROUPS' named entity 'ATP SYNTHASE' named entity 'ADJACENT' named entity 'NMR' named entity 'STATOR' named entity 'ROTOR' named entity 'INTERFACE' named entity 'MODEL OF' named entity 'FUNCTIONAL' named entity 'CYLINDRICAL' named entity 'PROTON TRANSFER' named entity 'ATP SYNTHASE' named entity 'MOLECULAR'

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