Pressure Adaptations in Deep-Sea <i>Moritella</i> Dihydrofolate Reductases: Compressibility versus Stability
Proteins from “pressure-loving” piezophiles appear to adapt by greater compressibility via larger total cavity volume. However, larger cavities in proteins have been associated with lower unfolding pressures. Here, dihydrofolate reductase (DHFR) from a moderate piezophile <i>Moritella profunda...
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| Format: | Article |
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MDPI AG
2021-11-01
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| Series: | Biology |
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| Online Access: | https://www.mdpi.com/2079-7737/10/11/1211 |
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| author | Ryan W. Penhallurick Toshiko Ichiye |
| author_facet | Ryan W. Penhallurick Toshiko Ichiye |
| author_sort | Ryan W. Penhallurick |
| collection | DOAJ |
| description | Proteins from “pressure-loving” piezophiles appear to adapt by greater compressibility via larger total cavity volume. However, larger cavities in proteins have been associated with lower unfolding pressures. Here, dihydrofolate reductase (DHFR) from a moderate piezophile <i>Moritella profunda</i> (Mp) isolated at ~2.9 km in depth and from a hyperpiezophile <i>Moritella yayanosii</i> (My) isolated at ~11 km in depth were compared using molecular dynamics simulations. Although previous simulations indicate that MpDHFR is more compressible than a mesophile DHFR, here the average properties and a quasiharmonic analysis indicate that MpDHFR and MyDHFR have similar compressibilities. A cavity analysis also indicates that the three unique mutations in MyDHFR are near cavities, although the cavities are generally similar in size in both. However, while a cleft overlaps an internal cavity, thus forming a pathway from the surface to the interior in MpDHFR, the unique residue Tyr103 found in MyDHFR forms a hydrogen bond with Leu78, and the sidechain separates the cleft from the cavity. Thus, while <i>Moritella</i> DHFR may generally be well suited to high-pressure environments because of their greater compressibility, adaptation for greater depths may be to prevent water entry into the interior cavities. |
| first_indexed | 2024-03-10T05:41:04Z |
| format | Article |
| id | doaj.art-3d535b27787c4d6f9c5a177425849307 |
| institution | Directory Open Access Journal |
| issn | 2079-7737 |
| language | English |
| last_indexed | 2024-03-10T05:41:04Z |
| publishDate | 2021-11-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Biology |
| spelling | doaj.art-3d535b27787c4d6f9c5a1774258493072023-11-22T22:28:59ZengMDPI AGBiology2079-77372021-11-011011121110.3390/biology10111211Pressure Adaptations in Deep-Sea <i>Moritella</i> Dihydrofolate Reductases: Compressibility versus StabilityRyan W. Penhallurick0Toshiko Ichiye1Department of Chemistry, Georgetown University, Washington, DC 20057, USADepartment of Chemistry, Georgetown University, Washington, DC 20057, USAProteins from “pressure-loving” piezophiles appear to adapt by greater compressibility via larger total cavity volume. However, larger cavities in proteins have been associated with lower unfolding pressures. Here, dihydrofolate reductase (DHFR) from a moderate piezophile <i>Moritella profunda</i> (Mp) isolated at ~2.9 km in depth and from a hyperpiezophile <i>Moritella yayanosii</i> (My) isolated at ~11 km in depth were compared using molecular dynamics simulations. Although previous simulations indicate that MpDHFR is more compressible than a mesophile DHFR, here the average properties and a quasiharmonic analysis indicate that MpDHFR and MyDHFR have similar compressibilities. A cavity analysis also indicates that the three unique mutations in MyDHFR are near cavities, although the cavities are generally similar in size in both. However, while a cleft overlaps an internal cavity, thus forming a pathway from the surface to the interior in MpDHFR, the unique residue Tyr103 found in MyDHFR forms a hydrogen bond with Leu78, and the sidechain separates the cleft from the cavity. Thus, while <i>Moritella</i> DHFR may generally be well suited to high-pressure environments because of their greater compressibility, adaptation for greater depths may be to prevent water entry into the interior cavities.https://www.mdpi.com/2079-7737/10/11/1211deep-sea adaptationscompressibilitycavitiespressurepotential energy landscape |
| spellingShingle | Ryan W. Penhallurick Toshiko Ichiye Pressure Adaptations in Deep-Sea <i>Moritella</i> Dihydrofolate Reductases: Compressibility versus Stability Biology deep-sea adaptations compressibility cavities pressure potential energy landscape |
| title | Pressure Adaptations in Deep-Sea <i>Moritella</i> Dihydrofolate Reductases: Compressibility versus Stability |
| title_full | Pressure Adaptations in Deep-Sea <i>Moritella</i> Dihydrofolate Reductases: Compressibility versus Stability |
| title_fullStr | Pressure Adaptations in Deep-Sea <i>Moritella</i> Dihydrofolate Reductases: Compressibility versus Stability |
| title_full_unstemmed | Pressure Adaptations in Deep-Sea <i>Moritella</i> Dihydrofolate Reductases: Compressibility versus Stability |
| title_short | Pressure Adaptations in Deep-Sea <i>Moritella</i> Dihydrofolate Reductases: Compressibility versus Stability |
| title_sort | pressure adaptations in deep sea i moritella i dihydrofolate reductases compressibility versus stability |
| topic | deep-sea adaptations compressibility cavities pressure potential energy landscape |
| url | https://www.mdpi.com/2079-7737/10/11/1211 |
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