2JGO

Structure of the arsenated de novo designed peptide Coil Ser L9C

Summary for 2JGO

• Entry DOI: 10.2210/pdb2jgo/pdb
• Descriptor: COIL SER L9C, ARSENIC, ZINC ION, ... (4 entities in total)
• Functional Keywords: de novo design, three-stranded coiled coil, arsenic(iii) binding protein, de novo protein
• Biological source: SYNTHETIC CONSTRUCT
• Total number of polymer chains: 3
• Total formula weight: 10314.11

Authors

Touw, D.S.,Nordman, C.E.,Stuckey, J.A.,Pecoraro, V.L. (deposition date: 2007-02-13, release date: 2007-07-10, Last modification date: 2024-11-13)

Primary citation

Touw, D.S.,Nordman, C.E.,Stuckey, J.A.,Pecoraro, V.L.
Identifying Important Structural Characteristics of Arsenic Resistance Proteins by Using Designed Three-Stranded Coiled Coils.
Proc.Natl.Acad.Sci.USA, 104:11969-, 2007

PubMed Abstract: Arsenic, a contaminant of water supplies worldwide, is one of the most toxic inorganic ions. Despite arsenic's health impact, there is relatively little structural detail known about its interactions with proteins. Bacteria such as Escherichia coli have evolved arsenic resistance using the Ars operon that is regulated by ArsR, a repressor protein that dissociates from DNA when As(III) binds. This protein undergoes a critical conformational change upon binding As(III) with three cysteine residues. Unfortunately, structures of ArsR with or without As(III) have not been reported. Alternatively, de novo designed peptides can bind As(III) in an endo configuration within a thiolate-rich environment consistent with that proposed for both ArsR and ArsD. We report the structure of the As(III) complex of Coil Ser L9C to a 1.8-A resolution, providing x-ray characterization of As(III) in a Tris thiolate protein environment and allowing a structural basis by which to understand arsenated ArsR.

PubMed: 17609383
DOI: 10.1073/PNAS.0701979104

Experimental method

X-RAY DIFFRACTION (1.81 Å)