Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Search research articles

Related Experiment Videos

Monellin (MNEI) at 1.15 A resolution.

J R Hobbs¹, S D Munger, G L Conn

¹Manchester Interdisciplinary Biocentre, Faculty of Life Sciences, University of Manchester, Manchester M60 1QD, England.

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications

|March 3, 2007

Summary

This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Bone Marrow Transplantation.

Bristol medico-chirurgical journal (1963)·2017

Same author

Immunological studies in chronic granulomatous candidiasis and the effect of treatment with dialysable transfer factor.

Archives of disease in childhood·2010

Same author

Congestive Cardiac Failure due to Secondary Amyloidosis.

Proceedings of the Royal Society of Medicine·2010

Same author

The receptor basis of sweet taste in mammals.

Results and problems in cell differentiation·2008

Same author

Further aspects of human immunoglobulin A deficiency.

Annals of clinical biochemistry·2007

Same author

Central role of the CNGA4 channel subunit in Ca2+-calmodulin-dependent odor adaptation.

Science (New York, N.Y.)·2001

Same journal

Overexpression, crystallization and preliminary X-ray crystallographic analysis of glucuronoxylan xylanohydrolase (Xyn30A) from Clostridium thermocellum.

Acta crystallographica. Section F, Structural biology and crystallization communications·2013

Same journal

Crystallization and preliminary X-ray diffraction analysis of D53H mutant Escherichia coli cAMP receptor protein.

Acta crystallographica. Section F, Structural biology and crystallization communications·2013

Same journal

Purification, crystallization and preliminary crystallographic analysis of the ligand-binding regions of the PctA and PctB chemoreceptors from Pseudomonas aeruginosa in complex with amino acids.

Acta crystallographica. Section F, Structural biology and crystallization communications·2013

Same journal

Expression, purification, crystallization and preliminary X-ray diffraction analysis of the aspartate transcarbamoylase domain of human CAD.

Acta crystallographica. Section F, Structural biology and crystallization communications·2013

Same journal

Cloning, expression, purification, crystallization and preliminary X-ray studies of argininosuccinate lyase (Rv1659) from Mycobacterium tuberculosis.

Acta crystallographica. Section F, Structural biology and crystallization communications·2013

Same journal

Expression, purification, crystallization and preliminary X-ray analysis of the receiver domain of Staphylococcus aureus LytR protein.

Acta crystallographica. Section F, Structural biology and crystallization communications·2013

See all related articles

The high-resolution X-ray structure of single-chain monellin (MNEI) reveals unique structural features and potential interactions with the sweet taste receptor. This finding advances our understanding of sweet taste perception.

Area of Science:

Structural Biology
Protein Crystallography
Molecular Interactions

Background:

Monellin is a natural sweet-tasting protein.
Previous structures of monellin showed a dimer interface, which was absent in this study.
Understanding MNEI structure is key to understanding sweet taste perception.

Purpose of the Study:

To determine the high-resolution X-ray crystal structure of single-chain monellin (MNEI).
To investigate the structural basis for MNEI's sweet taste.
To explore potential interactions between MNEI and the sweet taste receptor (T1R2-T1R3).

Main Methods:

X-ray crystallography at 1.15 A resolution.
Refinement using anisotropic displacement parameters and riding hydrogen atoms.

Related Experiment Videos

Analysis of protein structure, including side-chain conformations and bound ions.

Main Results:

A high-resolution (1.15 A) crystal structure of MNEI was obtained.
The structure lacked the previously observed dimer interface.
Detailed analysis revealed alternative side-chain conformations for 38 residues and four bound negative ions, suggesting electrostatic interactions with the T1R2-T1R3 receptor.

Conclusions:

The unique MNEI structure provides unprecedented detail.
The absence of a dimer interface may be a key feature of this monellin variant.
Bound ions offer new insights into MNEI's interaction with the sweet taste receptor, potentially explaining its function.