7KOS

1.50 Angstroms Resolution Crystal Structure of Putative Pterin Binding Protein PruR (Atu3496) from Agrobacterium fabrum str. C58

7KOS の概要

• エントリーDOI: 10.2210/pdb7kos/pdb
• 分子名称: Pterin Binding Protein, SODIUM ION, MALONIC ACID, ... (6 entities in total)
• 機能のキーワード: structural genomics, center for structural genomics of infectious diseases, csgid, prur, pterin binding protein
• 由来する生物種: Agrobacterium fabrum (strain C58 / ATCC 33970)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 66708.07

構造登録者

Minasov, G.,Shuvalova, L.,Dubrovska, I.,Pshenychnyi, S.,Endres, M.,Satchell, K.J.F.,Center for Structural Genomics of Infectious Diseases (CSGID) (登録日: 2020-11-09, 公開日: 2021-11-17, 最終更新日: 2026-04-01)

主引用文献

Greenwich, J.L.,Eagan, J.L.,Feirer, N.,Boswinkle, K.,Minasov, G.,Shuvalova, L.,Inniss, N.L.,Raghavaiah, J.,Ghosh, A.K.,Satchell, K.J.F.,Allen, K.D.,Fuqua, C.
Control of biofilm formation by an Agrobacterium tumefaciens pterin-binding periplasmic protein conserved among diverse Proteobacteria.
Proc.Natl.Acad.Sci.USA, 121:e2319903121-e2319903121, 2024

PubMed Abstract: Biofilm formation and surface attachment in multiple Alphaproteobacteria is driven by unipolar polysaccharide (UPP) adhesins. The pathogen produces a UPP adhesin, which is regulated by the intracellular second messenger cyclic diguanylate monophosphate (c-di-GMP). Prior studies revealed that DcpA, a diguanylate cyclase-phosphodiesterase, is crucial in control of UPP production and surface attachment. DcpA is regulated by PruR, a protein with distant similarity to enzymatic domains known to coordinate the molybdopterin cofactor (MoCo). Pterins are bicyclic nitrogen-rich compounds, several of which are produced via a nonessential branch of the folate biosynthesis pathway, distinct from MoCo. The pterin-binding protein PruR controls DcpA activity, fostering c-di-GMP breakdown and dampening its synthesis. Pterins are excreted, and we report here that PruR associates with these metabolites in the periplasm, promoting interaction with the DcpA periplasmic domain. The pteridine reductase PruA, which reduces specific dihydro-pterin molecules to their tetrahydro forms, imparts control over DcpA activity through PruR. Tetrahydromonapterin preferentially associates with PruR relative to other related pterins, and the PruR-DcpA interaction is decreased in a mutant. PruR and DcpA are encoded in an operon with wide conservation among diverse Proteobacteria including mammalian pathogens. Crystal structures reveal that PruR and several orthologs adopt a conserved fold, with a pterin-specific binding cleft that coordinates the bicyclic pterin ring. These findings define a pterin-responsive regulatory mechanism that controls biofilm formation and related c-di-GMP-dependent phenotypes in and potentially acts more widely in multiple proteobacterial lineages.

PubMed: 38870058
DOI: 10.1073/pnas.2319903121

実験手法

X-RAY DIFFRACTION (1.5 Å)