4ndt

Crystal structure of L. decastes alpha-galactosyl-binding lectin, orthorhombic crystal form

spinqualitylabelsall models 4ndt, resolution 1.03Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4ndt is a 1 chain structure with sequence from Lyophyllum decastes. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.03Å Ligands: SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function AGBL_LYODE Publication Abstract from PubMed The crystal structure of the alpha-galactosyl binding Lyophyllum decastes lectin (LDL) was determined to 1.0 A resolution by Sulfur-SAD (Single-wavelength Anomalous Diffraction). The 10 kDa protein exhibits no sequence similarity to any protein with known structure and adopts a unique lectin fold, where a core of two antiparallel beta-sheets at the heart of the homodimer is connected to the periphery of the structure by intramolecular disulfide bridges. This fold suggests that LDL is secreted, which sets it apart from other mushroom lectins. Structures of complexes between LDL and the ligands alpha-methylgalactoside and globotriose shed light on the binding specificity. Sequence comparison suggests a location and function of LDL and homologous proteins in or at the fungal cell wall. Structural comparison allows the identification of a superfamily of secreted proteins with the LDL fold, which may play a role at the interface between fungi and their environment. Atomic-resolution Structure of the alpha-galactosyl binding Lyophyllum decastes lectin reveals a new protein family found in both fungi and plants.,van Eerde A, Grahn EM, Winter HC, Goldstein IJ, Krengel U Glycobiology. 2014 Dec 11. pii: cwu136. PMID:25504801 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA