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Sulfate‐compatible density marks an intratrimeric junction in the Escherichia coli dihydrolipoamide succinyltransferase catalytic domain.

Bibliographic Details
Title: Sulfate‐compatible density marks an intratrimeric junction in the Escherichia coli dihydrolipoamide succinyltransferase catalytic domain.
Authors: Lim, Bison, Kim, Eunji, Byun, Jungeun, Kim, Minjeong, Kim, Hyo Jung
Source: Acta Crystallographica: Section F, Structural Biology Communications; Oct2026, Vol. 82 Issue 10, p362-368, 7p
Subject Terms: Crystal structure, Escherichia coli, Enzymes, Space groups
Abstract: The catalytic domain of Escherichia coli dihydrolipoamide succinyltransferase (EcDSCD), the E2 component of the 2‐oxoglutarate dehydrogenase complex, forms the oligomeric core of the multi‐enzyme assembly. Here, we report the crystal structure of EcDSCD determined in space group F432. The F432 crystal symmetry captures a compact trimeric building block and a symmetry‐expanded 24‐subunit assembly consistent with the octahedral architecture of the E2 catalytic core. Structural analysis revealed sulfate‐compatible electron density near Lys196 at a crystallographic threefold intratrimeric junction. Comparison with previously reported EcDSCD structures suggests that this density marks a structurally relevant oxyanion‐sensitive hotspot at the intratrimeric junction. Notably, the α1‐helix is positioned adjacent to the Lys196‐centered junction and extends towards the active‐site pocket, where it adopts a shifted orientation relative to other EcDSCD crystal forms. These observations link sulfate‐compatible density, the intratrimeric junction and α1‐helix positioning within the EcDSCD 24‐mer, providing a structural framework for understanding local oxyanion‐sensitive features in the E2 catalytic core. [ABSTRACT FROM AUTHOR]
Copyright of Acta Crystallographica: Section F, Structural Biology Communications is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
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  Data: Sulfate‐compatible density marks an intratrimeric junction in the Escherichia coli dihydrolipoamide succinyltransferase catalytic domain.
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  Data: <searchLink fieldCode="AR" term="%22Lim%2C+Bison%22">Lim, Bison</searchLink><br /><searchLink fieldCode="AR" term="%22Kim%2C+Eunji%22">Kim, Eunji</searchLink><br /><searchLink fieldCode="AR" term="%22Byun%2C+Jungeun%22">Byun, Jungeun</searchLink><br /><searchLink fieldCode="AR" term="%22Kim%2C+Minjeong%22">Kim, Minjeong</searchLink><br /><searchLink fieldCode="AR" term="%22Kim%2C+Hyo+Jung%22">Kim, Hyo Jung</searchLink>
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  Data: Acta Crystallographica: Section F, Structural Biology Communications; Oct2026, Vol. 82 Issue 10, p362-368, 7p
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  Data: <searchLink fieldCode="DE" term="%22Crystal+structure%22">Crystal structure</searchLink><br /><searchLink fieldCode="DE" term="%22Escherichia+coli%22">Escherichia coli</searchLink><br /><searchLink fieldCode="DE" term="%22Enzymes%22">Enzymes</searchLink><br /><searchLink fieldCode="DE" term="%22Space+groups%22">Space groups</searchLink>
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  Label: Abstract
  Group: Ab
  Data: The catalytic domain of Escherichia coli dihydrolipoamide succinyltransferase (EcDSCD), the E2 component of the 2‐oxoglutarate dehydrogenase complex, forms the oligomeric core of the multi‐enzyme assembly. Here, we report the crystal structure of EcDSCD determined in space group F432. The F432 crystal symmetry captures a compact trimeric building block and a symmetry‐expanded 24‐subunit assembly consistent with the octahedral architecture of the E2 catalytic core. Structural analysis revealed sulfate‐compatible electron density near Lys196 at a crystallographic threefold intratrimeric junction. Comparison with previously reported EcDSCD structures suggests that this density marks a structurally relevant oxyanion‐sensitive hotspot at the intratrimeric junction. Notably, the α1‐helix is positioned adjacent to the Lys196‐centered junction and extends towards the active‐site pocket, where it adopts a shifted orientation relative to other EcDSCD crystal forms. These observations link sulfate‐compatible density, the intratrimeric junction and α1‐helix positioning within the EcDSCD 24‐mer, providing a structural framework for understanding local oxyanion‐sensitive features in the E2 catalytic core. [ABSTRACT FROM AUTHOR]
– Name: Abstract
  Label:
  Group: Ab
  Data: <i>Copyright of Acta Crystallographica: Section F, Structural Biology Communications is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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        Value: 10.1107/S2053230X2600909X
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      – Code: eng
        Text: English
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        PageCount: 7
        StartPage: 362
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      – SubjectFull: Crystal structure
        Type: general
      – SubjectFull: Escherichia coli
        Type: general
      – SubjectFull: Enzymes
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      – SubjectFull: Space groups
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      – TitleFull: Sulfate‐compatible density marks an intratrimeric junction in the Escherichia coli dihydrolipoamide succinyltransferase catalytic domain.
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            – D: 01
              M: 10
              Text: Oct2026
              Type: published
              Y: 2026
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              Value: 82
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            – TitleFull: Acta Crystallographica: Section F, Structural Biology Communications
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