9JBD
Crystal Structure of the MoaE-like domain within Rv3323c from Mycobacterium tuberculosis
Summary for 9JBD
| Entry DOI | 10.2210/pdb9jbd/pdb |
| Descriptor | Probable MoaD-MoaE fusion protein MoaX, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | molybdopterin synthase, moax, transferase |
| Biological source | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
| Total number of polymer chains | 1 |
| Total formula weight | 16283.42 |
| Authors | |
| Primary citation | Cho, H.J.,Yang, S.H.,Lee, H.S.,Kang, B.S. Structural comparison of three MoaE proteins in Mycobacterium tuberculosis: Insights into molybdopterin synthase assembly and specificity. Biochem.Biophys.Res.Commun., 768:151945-151945, 2025 Cited by PubMed Abstract: Molybdoenzymes are essential for the survival and pathogenicity of Mycobacterium tuberculosis and require the molybdenum cofactor (MoCo). The biosynthesis of MoCo involves the molybdopterin (MPT) synthase complex, which is composed of the MoaD and MoaE subunits. The genome of M. tuberculosis encodes three homologs of MoaE: MoaE1, MoaE2, and MoaXE (the latter being a MoaE component of a MoaD-MoaE fusion protein known as MoaX), as well as three MoaD proteins. However, the structural basis for their functional specificity and interaction with MoaD partners remains unclear. We determined the crystal structures of all three MoaE proteins, revealing a conserved α/β hammerhead fold with distinct binding interface features resulting from minor sequence variations. Pull-down assays demonstrate that MoaE2 and MoaXE selectively interact with their cognate MoaD partners, while MoaE1 exhibits promiscuous binding to all MoaD forms. Although the structural plasticity of MoaE1 enables binding to three MoaD forms, it suggests that not all MoaE-MoaD combinations yield functional MPT synthase complexes, as structural rearrangements can lead to enzymatic inactivation. Our findings provide detailed insights into the molecular determinants that govern the assembly and specificity of MPT synthase in M. tuberculosis. PubMed: 40345009DOI: 10.1016/j.bbrc.2025.151945 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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