4tx4

Crystal Structure of a Single-Domain Cysteine Protease Inhibitor from Cowpea (Vigna unguiculata)

spinqualitylabelsall models 4tx4, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4tx4 is a 2 chain structure with sequence from Vigna unguiculata. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.95Å Ligands: SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CYTI_VIGUN Publication Abstract from PubMed Two cysteine proteinase inhibitors from cowpea, VuCys1 and VuCys2, were produced in E. coli ArcticExpress (DE3). The recombinant products strongly inhibited papain and chymopapain as well as the midgut proteases from Callosobruchus maculatus larvae, a bruchid that uses cysteine proteases as major digestive enzymes. Heat treatment at 100 degrees C for up to 60min or incubation at various pH values caused little reduction in the papain inhibitory activity of both inhibitors. Moreover, minor conformational variations, as probed by circular dichroism spectroscopy, were observed after VuCys1 and VuCys2 were subjected to these treatments. The crystal structure of VuCys1 was determined at a resolution of 1.95A, revealing a domain-swapped dimer in the asymmetric unit. However, the two lobes of the domain-swapped dimer are positioned closer to each other in VuCys1 in comparison to other similar cystatin structures. Moreover, some polar residues from opposite lobes recruit water molecules, forming a hydrogen bond network that mediates contacts between the lobes, thus generating an extended open interface. Due to the closer distance between the lobes, a small hydrophobic core is also formed, further stabilizing the folded domain-swapped dimer. These structural features might account for the extraordinary thermal and pH stability of VuCys1. Expression in Escherichia coli of cysteine protease inhibitors from cowpea (Vigna unguiculata): The crystal structure of a single-domain cystatin gives insights on its thermal and pH stability.,Monteiro Junior JE, Valadares NF, Pereira HD, Dyszy FH, da Costa Filho AJ, Uchoa AF, de Oliveira AS, da Silveira Carvalho CP, Grangeiro TB Int J Biol Macromol. 2017 Sep;102:29-41. doi: 10.1016/j.ijbiomac.2017.04.008., Epub 2017 Apr 4. PMID:28389401 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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