The structure of subunit E of the pyrococcus horikoshii OT3 A-ATP synthase gives insight into the elasticity of the peripheral stalk
A1AO ATP synthases are the major energy converters of archaea. They are composed of an A1 region that synthesizes ATP and an integral part AO that conducts ions. Subunit E is a component of the peripheral stalk that links the A1 with the AO part of the A-ATP synthase. We have determined the crystal...
| Main Authors: | , , |
|---|---|
| Other Authors: | |
| Format: | Journal Article |
| Language: | English |
| Published: |
2013
|
| Subjects: | |
| Online Access: | https://hdl.handle.net/10356/96161 http://hdl.handle.net/10220/11409 |
| _version_ | 1811686141233987584 |
|---|---|
| author | Balakrishna, Asha Manikkoth Hunke, Cornelia Grüber, Gerhard |
| author2 | School of Biological Sciences |
| author_facet | School of Biological Sciences Balakrishna, Asha Manikkoth Hunke, Cornelia Grüber, Gerhard |
| author_sort | Balakrishna, Asha Manikkoth |
| collection | NTU |
| description | A1AO ATP synthases are the major energy converters of archaea. They are composed of an A1 region that synthesizes ATP and an integral part AO that conducts ions. Subunit E is a component of the peripheral stalk that links the A1 with the AO part of the A-ATP synthase. We have determined the crystal structure of the entire subunit E (PhE) of the Pyrococcus horikoshii OT3 A-ATP synthase at 3.6 Å resolution. The structure reveals an extended S-shaped N-terminal α-helix with 112.29 Å in length, followed by a globular head group. The S-shaped feature, common in elastic connectors and spacers, would facilitate the storage of transient elastic energy during rotary motion in the enzyme. The structure has been superimposed into the asymmetric peripheral stalks of the three-dimensional reconstruction of the Pyrococcus furiosus enzyme, revealing that the S-shaped subunit PhE fits well into the bent peripheral stalk, whereas the previously solved E subunit structure (3.1 Å resolution) of Thermus thermophilus A-ATP synthase is well accommodated in the density of the straight stator domain. The different features of the two stalk subunits are discussed in light of a novel coupling mechanism in A-ATP synthases proposed to differ from the Wankel engine of F-ATP synthases. |
| first_indexed | 2024-10-01T04:55:42Z |
| format | Journal Article |
| id | ntu-10356/96161 |
| institution | Nanyang Technological University |
| language | English |
| last_indexed | 2024-10-01T04:55:42Z |
| publishDate | 2013 |
| record_format | dspace |
| spelling | ntu-10356/961612020-03-07T12:18:13Z The structure of subunit E of the pyrococcus horikoshii OT3 A-ATP synthase gives insight into the elasticity of the peripheral stalk Balakrishna, Asha Manikkoth Hunke, Cornelia Grüber, Gerhard School of Biological Sciences DRNTU::Science::Biological sciences A1AO ATP synthases are the major energy converters of archaea. They are composed of an A1 region that synthesizes ATP and an integral part AO that conducts ions. Subunit E is a component of the peripheral stalk that links the A1 with the AO part of the A-ATP synthase. We have determined the crystal structure of the entire subunit E (PhE) of the Pyrococcus horikoshii OT3 A-ATP synthase at 3.6 Å resolution. The structure reveals an extended S-shaped N-terminal α-helix with 112.29 Å in length, followed by a globular head group. The S-shaped feature, common in elastic connectors and spacers, would facilitate the storage of transient elastic energy during rotary motion in the enzyme. The structure has been superimposed into the asymmetric peripheral stalks of the three-dimensional reconstruction of the Pyrococcus furiosus enzyme, revealing that the S-shaped subunit PhE fits well into the bent peripheral stalk, whereas the previously solved E subunit structure (3.1 Å resolution) of Thermus thermophilus A-ATP synthase is well accommodated in the density of the straight stator domain. The different features of the two stalk subunits are discussed in light of a novel coupling mechanism in A-ATP synthases proposed to differ from the Wankel engine of F-ATP synthases. 2013-07-15T04:49:18Z 2019-12-06T19:26:27Z 2013-07-15T04:49:18Z 2019-12-06T19:26:27Z 2012 2012 Journal Article Balakrishna, A. M., Hunke, C., & Grüber, G. (2012). The Structure of Subunit E of the Pyrococcus horikoshii OT3 A-ATP Synthase Gives Insight into the Elasticity of the Peripheral Stalk. Journal of Molecular Biology, 420(3), 155-163. 0022-2836 https://hdl.handle.net/10356/96161 http://hdl.handle.net/10220/11409 10.1016/j.jmb.2012.04.012 en Journal of molecular biology © 2012 Elsevier Ltd. |
| spellingShingle | DRNTU::Science::Biological sciences Balakrishna, Asha Manikkoth Hunke, Cornelia Grüber, Gerhard The structure of subunit E of the pyrococcus horikoshii OT3 A-ATP synthase gives insight into the elasticity of the peripheral stalk |
| title | The structure of subunit E of the pyrococcus horikoshii OT3 A-ATP synthase gives insight into the elasticity of the peripheral stalk |
| title_full | The structure of subunit E of the pyrococcus horikoshii OT3 A-ATP synthase gives insight into the elasticity of the peripheral stalk |
| title_fullStr | The structure of subunit E of the pyrococcus horikoshii OT3 A-ATP synthase gives insight into the elasticity of the peripheral stalk |
| title_full_unstemmed | The structure of subunit E of the pyrococcus horikoshii OT3 A-ATP synthase gives insight into the elasticity of the peripheral stalk |
| title_short | The structure of subunit E of the pyrococcus horikoshii OT3 A-ATP synthase gives insight into the elasticity of the peripheral stalk |
| title_sort | structure of subunit e of the pyrococcus horikoshii ot3 a atp synthase gives insight into the elasticity of the peripheral stalk |
| topic | DRNTU::Science::Biological sciences |
| url | https://hdl.handle.net/10356/96161 http://hdl.handle.net/10220/11409 |
| work_keys_str_mv | AT balakrishnaashamanikkoth thestructureofsubuniteofthepyrococcushorikoshiiot3aatpsynthasegivesinsightintotheelasticityoftheperipheralstalk AT hunkecornelia thestructureofsubuniteofthepyrococcushorikoshiiot3aatpsynthasegivesinsightintotheelasticityoftheperipheralstalk AT grubergerhard thestructureofsubuniteofthepyrococcushorikoshiiot3aatpsynthasegivesinsightintotheelasticityoftheperipheralstalk AT balakrishnaashamanikkoth structureofsubuniteofthepyrococcushorikoshiiot3aatpsynthasegivesinsightintotheelasticityoftheperipheralstalk AT hunkecornelia structureofsubuniteofthepyrococcushorikoshiiot3aatpsynthasegivesinsightintotheelasticityoftheperipheralstalk AT grubergerhard structureofsubuniteofthepyrococcushorikoshiiot3aatpsynthasegivesinsightintotheelasticityoftheperipheralstalk |