Understanding substrate binding and the role of gatekeeping residues in PigC access tunnels
- 2 February 2021
- journal article
- research article
- Published by Royal Society of Chemistry (RSC) in Chemical Communications
- Vol. 57 (21), 2681-2684
- https://doi.org/10.1039/d0cc08226k
Abstract
Prodigiosin ligase PigC has been engineered by semi-rational design to accept short chain-pyrroles, providing molecular understanding of access tunnels and the substrate-binding pocket.Keywords
This publication has 30 references indexed in Scilit:
- ConSurf: Using Evolutionary Data to Raise Testable Hypotheses about Protein FunctionIsrael Journal of Chemistry, 2013
- CAVER 3.0: A Tool for the Analysis of Transport Pathways in Dynamic Protein StructuresPLoS Computational Biology, 2012
- Characterisation of PigC and HapC, the prodigiosin synthetases from Serratia sp. and Hahella chejuensis with potential for biocatalytic production of anticancer agentsChemical Science, 2011
- ConSurf 2010: calculating evolutionary conservation in sequence and structure of proteins and nucleic acidsNucleic Acids Research, 2010
- Chemoenzymatic synthesis of prodigiosin analogues—exploring the substrate specificity of PigCChemical Communications, 2008
- The biosynthesis and regulation of bacterial prodigininesNature Reviews Microbiology, 2006
- A Family of Evolution–Entropy Hybrid Methods for Ranking Protein Residues by ImportanceJournal of Molecular Biology, 2004
- Chemistry and Biology of Roseophilin and the Prodigiosin Alkaloids: A Survey of the Last 2500 YearsAngewandte Chemie, 2003
- An Evolutionary Trace Method Defines Binding Surfaces Common to Protein FamiliesJournal of Molecular Biology, 1996
- The Synthesis of ProdigiosinJournal of the American Chemical Society, 1962