7V4Y

TTHA1264/TTHA1265 complex

Summary for 7V4Y

• Entry DOI: 10.2210/pdb7v4y/pdb
• Descriptor: Zinc-dependent peptidase, Putative zinc protease, ZINC ION, ... (4 entities in total)
• Functional Keywords: complex, close conformation, hydrolase
• Biological source: Thermus thermophilus HB8; More
• Total number of polymer chains: 2
• Total formula weight: 93900.06

Authors

Xu, M.,Xu, Q.,Ran, T.,Wang, W.,Sun, B.,Wang, Q. (deposition date: 2021-08-16, release date: 2022-06-29, Last modification date: 2023-11-29)

Primary citation

Xu, M.,Xu, Q.,Wang, M.,Qiu, S.,Xu, D.,Zhang, W.,Wang, W.,He, J.,Wang, Q.,Ran, T.,Sun, B.
Crystal structures of TTHA1265 and TTHA1264/TTHA1265 complex reveal an intrinsic heterodimeric assembly.
Int.J.Biol.Macromol., 207:424-433, 2022

PubMed Abstract: Zinc peptidase M16 family members are widely distributed in most prokaryotic and eukaryotic organisms. M16 family has been divided into three subfamilies, M16A, M16B and M16C, based on sequence alignments and subunit connectivity. TTHA1264, an M16B protein found in Thermus thermophiles HB8, possesses an HXXEH motif essential for Zn binding and catalytic activity. TTHA1265 is another member of M16B, which lacks the metal-binding motif but with a conserved active-site R/Y pair commonly found in the C-terminal half of M16 enzymes. Sequence analysis showed that two genes coding for TTHA1264 and TTHA1265 assemble into a single operon in the bacterial genome. Here, we report the crystal structure of TTHA1265 and TTHA1264/TTHA1265 complex from T. thermophilus HB8. Interestingly, when TTHA1264 and TTHA1265 are present alone, TTHA1264 forms a monomer, TTHA1265 forms a homodimer, respectively. However, TTHA264 and TTHA1265 assembled into a heterodimeric complex, indicating that they prefer to form heterodimer. Biochemical data further confirmed the heterodimeric assembly indicating intrinsic heterodimeric assembly of TTHA1264 and TTHA1265. This property of TTHA1264 and TTHA1265 is consistent with the characteristics of the M16B family.

PubMed: 35276293
DOI: 10.1016/j.ijbiomac.2022.03.020

Experimental method

X-RAY DIFFRACTION (2.4 Å)