Characterization of Sfp, aBacillus subtilisPhosphopantetheinyl Transferase for Peptidyl Carrier Protein Domains in Peptide Synthetases†

Biochemistry ◽  
1998 ◽  
Vol 37 (6) ◽  
pp. 1585-1595 ◽  
Author(s):  
Luis E. N. Quadri ◽  
Paul H. Weinreb ◽  
Ming Lei ◽  
Michiko M. Nakano ◽  
Peter Zuber ◽  
...  
Keyword(s):  
Protein Domains ◽  
Carrier Protein ◽  
Peptide Synthetases

scholarly journals Intermediary conformations linked to the directionality of the aminoacylation pathway of nonribosomal peptide synthetases

2021 ◽  
Author(s):  
Florian Mayerthaler ◽  
Anna-Lena Feldberg ◽  
Jonas Alfermann ◽  
Xun Sun ◽  
Wieland Steinchen ◽  
...  
Keyword(s):  
Conformational Changes ◽  
Protein Domains ◽  
Carrier Protein ◽  
Nonribosomal Peptide ◽  
Nonribosomal Peptide Synthetases ◽  
Peptide Synthetases

In-solution analysis of conformational changes of NRPS adenylation and peptidyl-carrier protein domains under catalytic conditions reveals a new intermediary conformation.

scholarly journals Biophysical Characterization of Acyl Carrier Protein Domains from a Polyunsaturated Fatty Acid Synthase

2012 ◽  
Vol 26 (S1) ◽  
Author(s):  
Uldaeliz Trujillo Rodriguez ◽  
Delise Oyola-Robles ◽  
Stefan Arold ◽  
Fernando Alves De Melo ◽  
John E. Ladbury ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Polyunsaturated Fatty Acid ◽  
Fatty Acid Synthase ◽  
Acyl Carrier Protein ◽  
Protein Domains ◽  
Carrier Protein ◽  
Biophysical Characterization

scholarly journals The inherent flexibility of type I non-ribosomal peptide synthetase multienzymes drives their catalytic activities

Open Biology ◽  
2021 ◽  
Vol 11 (5) ◽  
pp. 200386
Author(s):  
Sarah Bonhomme ◽  
Andréa Dessen ◽  
Pauline Macheboeuf
Keyword(s):  
Protein Domains ◽  
Bioactive Metabolites ◽  
Carrier Protein ◽  
Type I ◽  
Peptide Synthetases ◽  
Catalytic Domains ◽  
Large Size ◽  
Peptide Synthetase ◽  
Modify Amino Acid ◽  
Conformational Rearrangements

Non-ribosomal peptide synthetases (NRPSs) are multienzymes that produce complex natural metabolites with many applications in medicine and agriculture. They are composed of numerous catalytic domains that elongate and chemically modify amino acid substrates or derivatives and of non-catalytic carrier protein domains that can tether and shuttle the growing products to the different catalytic domains. The intrinsic flexibility of NRPSs permits conformational rearrangements that are required to allow interactions between catalytic and carrier protein domains. Their large size coupled to this flexibility renders these multi-domain proteins very challenging for structural characterization. Here, we summarize recent studies that offer structural views of multi-domain NRPSs in various catalytically relevant conformations, thus providing an increased comprehension of their catalytic cycle. A better structural understanding of these multienzymes provides novel perspectives for their re-engineering to synthesize new bioactive metabolites.

scholarly journals Structural and bioinformatic characterization of anAcinetobacter baumanniitype II carrier protein

2014 ◽  
Vol 70 (6) ◽  
pp. 1718-1725 ◽  
Author(s):  
C. Leigh Allen ◽  
Andrew M. Gulick
Keyword(s):  
Protein Domain ◽  
Carrier Protein ◽  
Free Standing ◽  
Peptide Synthetases ◽  
Catalytic Domains ◽  
Single Protein ◽  
Domain Interactions ◽  
Partner Proteins ◽  
Precise Role

Microorganisms produce a variety of natural productsviasecondary metabolic biosynthetic pathways. Two of these types of synthetic systems, the nonribosomal peptide synthetases (NRPSs) and polyketide synthases (PKSs), use large modular enzymes containing multiple catalytic domains in a single protein. These multidomain enzymes use an integrated carrier protein domain to transport the growing, covalently bound natural product to the neighboring catalytic domains for each step in the synthesis. Interestingly, some PKS and NRPS clusters contain free-standing domains that interact intermolecularly with other proteins. Being expressed outside the architecture of a multi-domain protein, these so-called type II proteins present challenges to understand the precise role they play. Additional structures of individual and multi-domain components of the NRPS enzymes will therefore provide a better understanding of the features that govern the domain interactions in these interesting enzyme systems. The high-resolution crystal structure of a free-standing carrier protein fromAcinetobacter baumanniithat belongs to a larger NRPS-containing operon, encoded by the ABBFA_003406–ABBFA_003399 genes ofA. baumanniistrain AB307-0294, that has been implicated inA. baumanniimotility, quorum sensing and biofilm formation, is presented here. Comparison with the closest structural homologs of other carrier proteins identifies the requirements for a conserved glycine residue and additional important sequence and structural requirements within the regions that interact with partner proteins.

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