4HE7

Crystal Structure of Brazzein

Summary for 4HE7

• Entry DOI: 10.2210/pdb4he7/pdb
• Descriptor: Defensin-like protein, SODIUM ION (3 entities in total)
• Functional Keywords: sweet-tasting protein, plant protein
• Biological source: Pentadiplandra brazzeana
• Total number of polymer chains: 1
• Total formula weight: 6514.32

Authors

Nagata, K.,Hongo, N.,Kameda, Y.,Yamamura, A.,Sasaki, H.,Lee, W.C.,Ishikawa, K.,Suzuki, E.,Tanokura, M. (deposition date: 2012-10-03, release date: 2013-03-27, Last modification date: 2023-11-08)

Primary citation

Nagata, K.,Hongo, N.,Kameda, Y.,Yamamura, A.,Sasaki, H.,Lee, W.C.,Ishikawa, K.,Suzuki, E.,Tanokura, M.
The structure of brazzein, a sweet-tasting protein from the wild African plant Pentadiplandra brazzeana
Acta Crystallogr.,Sect.D, 69:642-647, 2013

PubMed Abstract: Brazzein is the smallest sweet-tasting protein and was isolated from the wild African plant Pentadiplandra brazzeana. The brazzein molecule consists of 54 amino-acid residues and four disulfide bonds. Here, the first crystal structure of brazzein is reported at 1.8 Å resolution and is compared with previously reported solution structures. Despite the overall structural similarity, there are several remarkable differences between the crystal and solution structures both in their backbone folds and side-chain conformations. Firstly, there is an additional α-helix in the crystal structure. Secondly, the atomic r.m.s.d.s between the corresponding C(α)-atom pairs are as large as 2.0-2.2 Å between the crystal and solution structures. Thirdly, the crystal structure exhibits a molecular shape that is similar but not identical to the solution structures. The crystal structure of brazzein reported here will provide additional information and further insights into the intermolecular interaction of brazzein with the sweet-taste receptor.

PubMed: 23519673
DOI: 10.1107/S0907444913001005

Experimental method

X-RAY DIFFRACTION (1.8 Å)