3pro

ALPHA-LYTIC PROTEASE COMPLEXED WITH C-TERMINAL TRUNCATED PRO REGION

spinqualitylabelsall models 3pro, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3pro is a 4 chain structure with sequence from Lysobacter enzymogenes. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Ligands: AES Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PRLA_LYSEN Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed While the majority of proteins fold rapidly and spontaneously to their native states, the extracellular bacterial protease alpha-lytic protease (alphaLP) has a t(1/2) for folding of approximately 2,000 years, corresponding to a folding barrier of 30 kcal mol(-1). AlphaLP is synthesized as a pro-enzyme where its pro region (Pro) acts as a foldase to stabilize the transition state for the folding reaction. Pro also functions as a potent folding catalyst when supplied as a separate polypeptide chain, accelerating the rate of alphaLP folding by a factor of 3 x 10(9). In the absence of Pro, alphaLP folds only partially to a stable molten globule-like intermediate state. Addition of Pro to this intermediate leads to rapid formation of native alphaLP. Here we report the crystal structures of Pro and of the non-covalent inhibitory complex between Pro and native alphaLP. The C-shaped Pro surrounds the C-terminal beta-barrel domain of the folded protease, forming a large complementary interface. Regions of extensive hydration in the interface explain how Pro binds tightly to the native state, yet even more tightly to the folding transition state. Based on structural and functional data we propose that a specific structural element in alphaLP is largely responsible for the folding barrier and suggest how Pro can overcome this barrier. Structure of alpha-lytic protease complexed with its pro region.,Sauter NK, Mau T, Rader SD, Agard DA Nat Struct Biol. 1998 Nov;5(11):945-50. PMID:9808037 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Alpha-lytic protease Alpha-lytic protease 3D structures

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