4F6L

Crystal structure of Aureusimine biosynthetic cluster reductase domain

Summary for 4F6L

• Entry DOI: 10.2210/pdb4f6l/pdb
• Related: 4F6C
• Descriptor: AusA reductase domain protein (1 entity in total)
• Functional Keywords: thioester reductase, oxidoreductase
• Biological source: Staphylococcus aureus
• Total number of polymer chains: 2
• Total formula weight: 116140.98

Authors

Mok, M.,Junop, M. (deposition date: 2012-05-14, release date: 2012-12-12, Last modification date: 2024-02-28)

Primary citation

Wyatt, M.A.,Mok, M.C.,Junop, M.,Magarvey, N.A.
Heterologous expression and structural characterisation of a pyrazinone natural product assembly line.
Chembiochem, 13:2408-2415, 2012

PubMed Abstract: Through a number of strategies nonribosomal peptide assembly lines give rise to a metabolic diversity not possible by ribosomal synthesis. One distinction within nonribosomal assembly is that products are elaborated on an enzyme-tethered substrate, and their release is enzyme catalysed. Reductive release by NAD(P)H-dependent catalysts is one observed nonribosomal termination and release strategy. Here we probed the selectivity of a terminal reductase domain by using a full-length heterologously expressed nonribosomal peptide synthetase for the dipeptide aureusimine and were able to generate 17 new analogues. Further, we generated an X-ray structure of aureusimine terminal reductase to gain insight into the structural details associated with this enzymatic domain.

PubMed: 23070851
DOI: 10.1002/cbic.201200340

Experimental method

X-RAY DIFFRACTION (3.856 Å)