The structural basis of a high affinity ATP binding epsilon subunit froma bacterial ATP synthase

Collection with item attached
2017
Item details URL
http://open-repository.kisti.re.kr/cube/handle/open_repository/486140.do
DOI
10.1371/journal.pone.0177907
Title
The structural basis of a high affinity ATP binding epsilon subunit froma bacterial ATP synthase
Description
AK was supported by a Postdoctoral Fellowship for Foreign Researchersfrom the Japan Society for the Promotion of Science (JSPS-ID: P13705)(https://www.jsps.go.ip/). Computational resources have been provided bythe Okazaki Research Centre for Computational Sciences (to ST;https://ccportal.ims.ac.jp/en/). Part of this work was supported by JSPSKAKENHI (15K07013 to YKY). The funders had no role in study design, datacollection and analysis, decision to publish, or preparation of themanuscript.
abstract
The epsilon subunit from bacterial ATP synthases functions as an ATP sensor, preventing ATPase activity when the ATP concentration in bacterial cells crosses a certain threshold. The R103A/R115A double mutant of the e subunit from thermophilic Bacillus PS3 has been shown to bind ATP two orders of magnitude stronger than the wild type protein. We use molecular dynamics simulations and free energy calculations to derive the structural basis of the high affinity ATP binding to the R103A/R115A double mutant. Our results suggest that the double mutant is stabilized by an enhanced hydrogen-bond network and fewer repulsive contacts in the ligand binding site. The inferred structural basis of the high affinity mutant may help to design novel nucleotide sensors based on the e subunit from bacterial ATP synthases.
provenance
Made available in Cube on 2018-09-28T15:59:36Z (GMT). No. of bitstreams: 0
language
English
author
Krah, Alexander
Kato-Yamada, Yasuyuki
Takada, Shoji
orcid
Krah, Alexander/0000-0001-8871-5550
accessioned
2018-09-28T15:59:36Z
available
2018-09-28T15:59:36Z
issued
2017
citation
PLOS ONE(12): 5
issn
1932-6203
uri
http://open-repository.kisti.re.kr/cube/handle/open_repository/486140.do
Funder
과학기술정보통신부
Funding Program
한국고등과학원연구운영비지원
Project ID
1711061613
Jurisdiction
Rep.of Korea
Project Name
Understanding structure, selectivity and mechanism of the ATP synthase and drug transporters - Biological, medical and biotechnological implications
rights
openAccess
type
article


Files in This Item

There are no attached files.