21dh | pdb_000021dh

Crystal structure of MBP-fused Monobody P' in complex with HPPU

spinqualitylabelsall models 21dh, resolution 2.57Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 21dh is a 6 chain structure with sequence from Escherichia coli K-12 and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.57Å Ligands: A1MC1, BGC, GLC, PRD_900018 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MALE_ECOLI Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides. Publication Abstract from PubMed Monobodies, engineered protein scaffolds derived from the fibronectin type III domain, are powerful alternatives to conventional antibodies. While the native scaffold is robust, engineering the variable loops can often compromise solubility and promote aggregation. Here, we report the crystallization and structure determination at 2.57 A resolution of a monobody (Mb-P') engineered to bind the synthetic small molecule HPPU [1-(4-hydroxyphenyl)-3-phenylurea] with nanomolar affinity. Although Mb-P' exhibited severe polydispersity and heterogeneous oligomerization in solution, N-terminal fusion with maltose-binding protein (MBP) using an optimized linker successfully yielded monodisperse species and diffraction-quality crystals. The crystal structure exhibited pseudo-D(3) symmetry in the asymmetric unit, in which the MBP moiety interacts with and partially covers the F and G beta-strands of the monobody. This steric masking suggests that MBP acts as a solubility enhancer by shielding the aggregation-prone surface patches generated by loop engineering. Our results demonstrate that this fusion strategy effectively enables structural studies of aggregation-prone proteins obtained from engineered scaffolds. Crystallization and X-ray structure of a highly aggregation-prone monobody engineered for high-affinity small-molecule recognition.,Endo K, Umemoto S, Tsuzuki N, Okumura H, Sato Y, Yoshii T, Tsukiji S, Nagano S, Murakami H, Hino T Acta Crystallogr F Struct Biol Commun. 2026 Mar 1;82(Pt 3):75-82. doi: , 10.1107/S2053230X26000798. Epub 2026 Feb 9. PMID:41660693 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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