6KRB

High resolution crystal structure of an Acylphosphatase protein cage

Summary for 6KRB

• Entry DOI: 10.2210/pdb6krb/pdb
• Descriptor: Acylphosphatase, SULFATE ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: acylphosphatase, hydrolase
• Biological source: Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)
• Total number of polymer chains: 12
• Total formula weight: 129271.24

Authors

Chatterjee, S.,Nath, S.,Sen, U. (deposition date: 2019-08-21, release date: 2020-05-13, Last modification date: 2023-11-22)

Primary citation

Chatterjee, S.,Nath, S.,Sen, U.
High resolution structure of Vibrio cholerae acylphosphatase (VcAcP) cage: Identification of drugs, location of its binding site and engineering to facilitate cage formation.
Biochem.Biophys.Res.Commun., 523:348-353, 2020

PubMed Abstract: Protein cages have recently emerged as an extraordinary drug-delivery system due to its biocompatibility, biodegradability, low toxicity, ease to manipulate and engineer. We have reported earlier the formation and architecture of a do-decameric cage-like architecture of Vibrio cholerae acylphosphatase (VcAcP) at 3.1 Å. High resolution (2.4 Å) crystal structure of VcAcP cage, reported here, illuminates a potential binding site for sulphate/phosphate containing drugs whereas analysis of its subunit association and interfaces indicates high potential for cage engineering. Tryptophan quenching studies indeed discloses noteworthy binding with various sulphate/phosphate containing nucleotide-based drugs and vitamin B (PLP) demonstrating that exterior surface of VcAcP protein cage can be exploited as multifunctional carrier. Moreover, a quadruple mutant L30C/T68C/N40C/L81C-VcAcP (QM-VcAcP) capable to form an intricate disulphide bonded VcAcP cage has been designed. SEC, SDS-PAGE analysis and DLS experiment confirmed cysteine mediated engineered VcAcP cage formation.

PubMed: 31866010
DOI: 10.1016/j.bbrc.2019.12.060

Experimental method

X-RAY DIFFRACTION (2.375 Å)