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6QPR

Rhizomucor miehei lipase propeptide complex, Ser95/Ile96 deletion mutant

Summary for 6QPR
Entry DOI10.2210/pdb6qpr/pdb
DescriptorLipase, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
Functional Keywordslipase, propeptide, intramolecular chaperone, inhibition, deletion mutant, fungal, hydrolase
Biological sourceRhizomucor miehei
Total number of polymer chains1
Total formula weight39652.32
Authors
Moroz, O.V.,Blagova, E.,Reiser, V.,Saikia, R.,Dalal, S.,Jorgensen, C.I.,Baunsgaard, L.,Andersen, B.,Svendsen, A.,Wilson, K.S. (deposition date: 2019-02-14, release date: 2019-03-13, Last modification date: 2024-11-20)
Primary citationMoroz, O.V.,Blagova, E.,Reiser, V.,Saikia, R.,Dalal, S.,Jorgensen, C.I.,Bhatia, V.K.,Baunsgaard, L.,Andersen, B.,Svendsen, A.,Wilson, K.S.
Novel Inhibitory Function of theRhizomucor mieheiLipase Propeptide and Three-Dimensional Structures of Its Complexes with the Enzyme.
Acs Omega, 4:9964-9975, 2019
Cited by
PubMed Abstract: 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 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.
PubMed: 31460089
DOI: 10.1021/acsomega.9b00612
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.45 Å)
Structure validation

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