6qpr

Rhizomucor miehei lipase propeptide complex, Ser95/Ile96 deletion mutant

spinqualitylabelsall models 6qpr, resolution 1.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6qpr is a 1 chain structure with sequence from Rhizomucor miehei. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.45Å Ligands: NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function LIP_RHIMI Publication Abstract from PubMed Many proteins are synthesized as precursors, with propeptides playing a variety of roles such as assisting in folding or preventing them from being active within the cell. While the precise role of the propeptide in fungal lipases is not completely understood, it was previously reported that mutations in the propeptide region of the Rhizomucor miehei lipase have an influence on the activity of the mature enzyme, stressing the importance of the amino acid composition of this region. We here report two structures of this enzyme in complex with its propeptide, which suggests that the latter plays a role in the correct maturation of the enzyme. Most importantly, we demonstrate that the propeptide shows inhibition of lipase activity in standard lipase assays and propose that an important role of the propeptide is to ensure that the enzyme is not active during its expression pathway in the original host. Novel Inhibitory Function of the Rhizomucor miehei Lipase Propeptide and Three-Dimensional Structures of Its Complexes with the Enzyme.,Moroz OV, Blagova E, Reiser V, Saikia R, Dalal S, Jorgensen CI, Bhatia VK, Baunsgaard L, Andersen B, Svendsen A, Wilson KS ACS Omega. 2019 Jun 7;4(6):9964-9975. doi: 10.1021/acsomega.9b00612. eCollection , 2019 Jun 30. PMID:31460089 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Lipase 3D Structures

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