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Updated: Sep 30, 2025

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
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X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

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Crystal structures of TTHA1265 and TTHA1264/TTHA1265 complex reveal an intrinsic heterodimeric assembly

Mengxue Xu1, Qin Xu2, Meitian Wang3

  • 1Shanghai Institute of Applied Physics, Chinese Academy of Sciences, Shanghai 201800, China.; Department of Microbiology, College of Life Sciences, Nanjing Agricultural University, 210095 Nanjing, China.

International Journal of Biological Macromolecules
|March 11, 2022
PubMed

Insights

The M16B family zinc peptidases TTHA1264 and TTHA1265 from Thermus thermophilus HB8 preferentially form heterodimers. This structural finding reveals a unique assembly mechanism for these bacterial enzymes.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Microbiology

Background:

  • The M16 family of zinc peptidases is crucial in various organisms.
  • This family is classified into M16A, M16B, and M16C subfamilies.
  • TTHA1264 contains a key metal-binding motif, while TTHA1265 has a conserved active-site residue.

Purpose of the Study:

  • To elucidate the crystal structure of TTHA1265 and the TTHA1264/TTHA1265 complex.
  • To investigate the assembly properties of TTHA1264 and TTHA1265.

Main Methods:

  • X-ray crystallography
  • Protein expression and purification
  • Biochemical assays

Main Results:

  • TTHA1264 forms a monomer and TTHA1265 forms a homodimer in isolation.
  • TTHA1264 and TTHA1265 assemble into a stable heterodimeric complex.
  • Biochemical data confirm the intrinsic preference for heterodimerization.

Conclusions:

  • TTHA1264 and TTHA1265 exhibit a strong preference for forming heterodimers.
  • This heterodimeric assembly is consistent with the known characteristics of the M16B subfamily.
  • The findings provide structural insights into M16B enzyme function.
Keywords:
Crystal structureIntrinsic heterodimerM16 familyTTHA1264TTHA1265

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