3m7q | pdb_00003m7q

Crystal structure of recombinant Kunitz Type serine protease Inhibitor-1 from the Caribbean sea anemone stichodactyla helianthus in complex with bovine pancreatic trypsin

spinqualitylabelsall models 3m7q, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3m7q is a 2 chain structure with sequence from Bos taurus and Stihl. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: PO4 Activity: Trypsin, with EC number 3.4.21.4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [ISH1_STOHE] Active against serine, cysteine, and aspartic proteinases. Can bind vertebrate trypsin and chymotrypsin. Publication Abstract from PubMed Proteins isolated from marine invertebrates are frequently characterized by exceptional structural and functional properties. ShPI-1, a BPTI Kunitz-type inhibitor from the Caribbean Sea anemone Stichodactyla helianthus, displays activity not only against serine-, but also against cysteine-, and aspartate proteases. As an initial step to evaluate the molecular basis of its activities, we describe the crystallographic structure of ShPI-1 in complex with the serine protease bovine pancreatic trypsin at 1.7A resolution. The overall structure and the important enzyme-inhibitor interactions of this first invertebrate BPTI-like Kunitz-type inhibitor:trypsin complex remained largely conserved compared to mammalian BPTI-Kunitz inhibitor complexes. However, a prominent stabilizing role within the interface was attributed to arginine at position P3. Binding free-energy calculations indicated a 10-fold decrease for the inhibitor affinity against trypsin, if the P3 residue of ShPI-1 is mutated to alanine. Together with the increased role of Arg(11) at P3 position, slightly reduced interactions at the prime side (Pn') of the primary binding loop and at the secondary binding loop of ShPI-1 were detected. In addition, the structure provides important information for site directed mutagenesis to further optimize the activity of rShPI-1A for biotechnological applications. Structural insights into serine protease inhibition by a marine invertebrate BPTI Kunitz-type inhibitor.,Garcia-Fernandez R, Pons T, Perbandt M, Valiente PA, Talavera A, Gonzalez-Gonzalez Y, Rehders D, Chavez MA, Betzel C, Redecke L J Struct Biol. 2012 Sep 5. pii: S1047-8477(12)00240-7. doi:, 10.1016/j.jsb.2012.08.009. PMID:22975140 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Trypsin 3D structures

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