2WQT

Dodecahedral assembly of MhpD

Summary for 2WQT

• Entry DOI: 10.2210/pdb2wqt/pdb
• Related: 1SV6
• Descriptor: 2-KETO-4-PENTENOATE HYDRATASE, PHOSPHATE ION, SODIUM ION, ... (5 entities in total)
• Functional Keywords: lyase, hydratase, dodecahedral form, aromatic hydrocarbons catabolism
• Biological source: ESCHERICHIA COLI
• Total number of polymer chains: 20
• Total formula weight: 585510.38

Authors

Montgomery, M.G.,Wood, S.P. (deposition date: 2009-08-27, release date: 2010-01-19, Last modification date: 2023-12-20)

Primary citation

Montgomery, M.G.,Coker, A.R.,Taylor, I.A.,Wood, S.P.
Assembly of a 20Nm Protein Cage by Escherichia Coli 2-Hydroxypentadienoic Acid Hydratase (Mhpd).
J.Mol.Biol., 396:1379-, 2010

PubMed Abstract: The pentameric Escherichia coli enzyme 2-hydroxypentadienoic acid hydratase assembles to form a 20-nm-diameter particle comprising 60 protein subunits, arranged with 532 symmetry when crystallised at low pH in the presence of phosphate or sulphate ions. The particles form rapidly and are stable in solution during gel filtration at low pH. They are probably formed through trimers of pentamers, which are stabilised by the interaction of two phosphate ions with residues of the N-terminal domains of subunits at the 3-fold axis. Once the particles are formed at high concentrations of phosphate (or sulphate), they remain stable in solution at 20-fold lower concentrations of the anion. Guest molecules can be trapped within the hollow protein shell during assembly. The C-termini of the subunits are freely accessible on the surface of the protein cage and thus are ideal sites for addition of affinity tags or other modifications. These particles offer a convenient model system for studying the assembly of large symmetrical structures and a novel protein nanoparticle for encapsulation and cargo delivery.

PubMed: 20053352
DOI: 10.1016/J.JMB.2009.12.056

Experimental method

X-RAY DIFFRACTION (2.8 Å)