2015
DOI: 10.1074/jbc.m115.677492
|View full text |Cite
|
Sign up to set email alerts
|

Structural Basis for a Unique ATP Synthase Core Complex from Nanoarcheaum equitans

Abstract: Background: Structural asymmetry upon nucleotide binding is crucial for catalytic activity of ATP synthases. Results: The structures of apo and bound A 3 B 3 hexamer of N. equitans ATP synthase show conformational inflexibility. Conclusion: The N. equitans A 3 B 3 hexamer is an inactive form. Significance: The structure of inactive form of N. equitans ATP synthase A 3 B 3 is shown for the first time.

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1
1

Citation Types

0
12
0

Year Published

2016
2016
2019
2019

Publication Types

Select...
5
2

Relationship

0
7

Authors

Journals

citations
Cited by 15 publications
(12 citation statements)
references
References 73 publications
0
12
0
Order By: Relevance
“…The genome of N. equitans encodes an incomplete ATP synthase, which, even though shown to be expressed, has not been demonstrated to either generate or hydrolyze ATP 17 40 . Structural analysis of the core complex (A–B subunits) further suggests the N. equitans ATP synthase is inactive 41 . While the ATP synthase is absent in some insect and plant endosymbiotic or parasitic bacteria with extremely reduced genomes 42 43 44 , these organisms retain respiratory complexes to provide energy and maintain a polarized membrane.…”
Section: Resultsmentioning
confidence: 99%
“…The genome of N. equitans encodes an incomplete ATP synthase, which, even though shown to be expressed, has not been demonstrated to either generate or hydrolyze ATP 17 40 . Structural analysis of the core complex (A–B subunits) further suggests the N. equitans ATP synthase is inactive 41 . While the ATP synthase is absent in some insect and plant endosymbiotic or parasitic bacteria with extremely reduced genomes 42 43 44 , these organisms retain respiratory complexes to provide energy and maintain a polarized membrane.…”
Section: Resultsmentioning
confidence: 99%
“…Although several DPANN archaea encode subunits of putative ATP synthases, these protein complexes might not always be functional as suggested by the structural and biophysical investigations of the A 3 B 3 core complex of N. equitans (Mohanty et al. 2015). Yet, some genomes assigned to Parvarchaeota and Micrarchaeota have been reported to encode putative components of an aerobic electron transport chain and a canonical A-type ATP synthase besides the fermentation pathways common to most DPANN, which indicate an ability for both aerobic and anaerobic metabolism (Baker et al.…”
Section: What Is Encoded By the Small Genomes Of Dpann Archaea?mentioning
confidence: 99%
“…Furthermore, the likely inactive ATPase of N. equitans raises the question of how it obtains ATP (Lewalter and Müller 2006; Mohanty et al. 2015). The unique membrane system of I. hospitalis , consisting of an inner- and outer membrane separated by a large periplasmic space and being one of the few examples of an energy-conserving outer membrane, is debated to play an essential role in energy conservation of N. equitans (Küper et al.…”
Section: Host–symbiont Systems Involving Dpann Archaeamentioning
confidence: 99%
See 1 more Smart Citation
“…The most genome-reduced Archaea belong to the DPANN superphylum among which the ectoparasitic Nanoarchaeota and Huberarchaea have the smallest known genomes. For example, the genomes of N. equitans [57] and its close relative Nanopusillus acidilobi [58] are only 490 and 606 kb in size, respectively, and lack genes for various anabolic and catabolic pathways including a functional ATP synthase [58,59]. In general, members of the DPANN have genomes ranging from ∼0.5 to 1.5 Mb in size and many representatives lack genes for central carbon and energy metabolism.…”
Section: Genomic Features Of Archaeal Symbionts?mentioning
confidence: 99%