Structural determination of the active site of a sweet protein. A 1H NMR investigation of pMNEI.

Abstract:

:pMNEI, a single chain sweet protein related to monellin, has been studied by means of 1H NMR at 500 MHz. A partial sequential assignment performed by means of the MCD method allowed the determination of the secondary structure of a large portion of the beta-sheet of pMNEI that contains a likely 'sweet finger': the loop connecting the beta-strands from residue 59 to residue 78, corresponding to segment 16-35 of the A chain of monellin. The detailed three-dimensional structure of the loop (Tyr66-Ala67-Ser68-Asp69), determined from several interresidue and intraresidue NOEs and subsequent energy minimization, shows that the side chains of Tyr66 and Asp69 fit our model of the sweet receptor in a manner very similar to that of the side chains of Phe and Asp of aspartame.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Tancredi T,Iijima H,Saviano G,Amodeo P,Temussi PA

doi

10.1016/0014-5793(92)81138-c

keywords:

subject

Has Abstract

pub_date

1992-09-21 00:00:00

pages

27-30

issue

1

eissn

0014-5793

issn

1873-3468

pii

0014-5793(92)81138-C

journal_volume

310

pub_type

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