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7REO

Crystal structure of an engineered variant of single-chain Penicillin G Acylase from Kluyvera cryocrescens (global hydrolysis Rd3CHis)

Summary for 7REO
Entry DOI10.2210/pdb7reo/pdb
DescriptorPenicillin G Acylase, CALCIUM ION (3 entities in total)
Functional Keywordspenicillin, acylase, hydrolase
Biological sourceKluyvera cryocrescens
Total number of polymer chains1
Total formula weight86206.26
Authors
Orth, P. (deposition date: 2021-07-13, release date: 2021-11-17, Last modification date: 2023-10-18)
Primary citationFryszkowska, A.,An, C.,Alvizo, O.,Banerjee, G.,Canada, K.A.,Cao, Y.,DeMong, D.,Devine, P.N.,Duan, D.,Elgart, D.M.,Farasat, I.,Gauthier, D.R.,Guidry, E.N.,Jia, X.,Kong, J.,Kruse, N.,Lexa, K.W.,Makarov, A.A.,Mann, B.F.,Milczek, E.M.,Mitchell, V.,Nazor, J.,Neri, C.,Orr, R.K.,Orth, P.,Phillips, E.M.,Riggins, J.N.,Schafer, W.A.,Silverman, S.M.,Strulson, C.A.,Subramanian, N.,Voladri, R.,Yang, H.,Yang, J.,Yi, X.,Zhang, X.,Zhong, W.
A chemoenzymatic strategy for site-selective functionalization of native peptides and proteins.
Science, 376:1321-1327, 2022
Cited by
PubMed Abstract: The emergence of new therapeutic modalities requires complementary tools for their efficient syntheses. Availability of methodologies for site-selective modification of biomolecules remains a long-standing challenge, given the inherent complexity and the presence of repeating residues that bear functional groups with similar reactivity profiles. We describe a bioconjugation strategy for modification of native peptides relying on high site selectivity conveyed by enzymes. We engineered penicillin G acylases to distinguish among free amino moieties of insulin (two at amino termini and an internal lysine) and manipulate cleavable phenylacetamide groups in a programmable manner to form protected insulin derivatives. This enables selective and specific chemical ligation to synthesize homogeneous bioconjugates, improving yield and purity compared to the existing methods, and generally opens avenues in the functionalization of native proteins to access biological probes or drugs.
PubMed: 35709255
DOI: 10.1126/science.abn2009
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.812 Å)
Structure validation

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