2O9U

Monellin (MNEI) at 1.15 resolution

Summary for 2O9U

• Entry DOI: 10.2210/pdb2o9u/pdb
• Descriptor: Monellin chain B and Monellin chain A, SULFATE ION (3 entities in total)
• Functional Keywords: alternative conformations, 3-10 polyproline ii helix, plant protein
• Biological source: Dioscoreophyllum cumminsii (serendipity berry); More
• Total number of polymer chains: 1
• Total formula weight: 11803.30

Authors

Hobbs, J.R.,Munger, S.D.,Conn, G.L. (deposition date: 2006-12-14, release date: 2007-02-20, Last modification date: 2023-10-25)

Primary citation

Hobbs, J.R.,Munger, S.D.,Conn, G.L.
Monellin (MNEI) at 1.15 A resolution
Acta Crystallogr.,Sect.F, 63:162-167, 2007

PubMed Abstract: The X-ray crystal structure of a single-chain monellin protein (MNEI) has been determined at 1.15 A resolution. The model was refined to convergence employing anisotropic displacement parameters and riding H atoms to produce a final model with R(work) and R(free) values of 0.132 and 0.162, respectively. The crystal contains a single MNEI protein in the asymmetric unit and unusually lacks the dimer interface observed in all previous crystal structures of monellin and its single-chain derivatives. The high resolution allowed a more detailed view of MNEI than previously possible, with 38 of the 96 residues modelled with alternative side-chain conformations, including four core residues Thr12, Cys41, Leu62 and Ile75. Four stably bound negative ions were also located, providing new insight into potential electrostatic interactions of MNEI with the largely negatively charged surface of the sweet taste receptor T1R2-T1R3.

PubMed: 17329805
DOI: 10.1107/S1744309107005271

Experimental method

X-RAY DIFFRACTION (1.15 Å)