PDBsum entry 1bk8

Plant defensin

PDB id

1bk8

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Contents

			Protein chain

					50 a.a. *

* Residue conservation analysis

PDB id:

1bk8

Links
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- CATH
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Name:

Plant defensin

Title:

Determination of the three-dimensional solution structure of aesculus hippocastanum antimicrobial protein 1 (ah-amp1) by 1h nmr, 25 structures

Structure:

Antimicrobial protein 1. Chain: a. Synonym: ah-amp1

Source:

Aesculus hippocastanum. Common horse chestnut. Organism_taxid: 43364. Organ: seed

NMR struc:

25 models

Authors:

F.Fant,F.A.M.Borremans

Key ref:

F.Fant et al. (1999). The three-dimensional solution structure of Aesculus hippocastanum antimicrobial protein 1 determined by 1H nuclear magnetic resonance. Proteins, 37, 388-403. PubMed id: 10591099 DOI: 10.1002/(SICI)1097-0134(19991115)37:3<388::AID-PROT7>3.3.CO;2-6

Date:

15-Jul-98

Release date:

05-Jan-00

PROCHECK

	Headers

	References

Protein chain

Q7M1F3 (DEF1_AESHI) - Defensin-like protein 1 from Aesculus hippocastanum

Seq: Struc:					50 a.a. 50 a.a.

Key:

PfamA domain

Secondary structure

CATH domain

DOI no: 10.1002/(SICI)1097-0134(19991115)37:3<388::AID-PROT7>3.3.CO;2-6	Proteins 37:388-403 (1999)
PubMed id: 10591099

The three-dimensional solution structure of Aesculus hippocastanum antimicrobial protein 1 determined by 1H nuclear magnetic resonance.
F.Fant, W.F.Vranken, F.A.Borremans.

ABSTRACT

Aesculus hippocastanum antimicrobial protein 1 (Ah-AMP1) is a plant defensin isolated from horse chestnuts. The plant defensins have been divided in several subfamilies according to their amino acid sequence homology. Ah-AMP1, belonging to subfamily A2, inhibits growth of a broad range of fungi. So far, a three-dimensional structure has been determined only for members of subfamilies A3 and B2. In order to understand activity and specificity of these plant defensins, the structure of a protein belonging to subfamily A2 is needed. We report the three-dimensional solution structure of Ah-AMP1 as determined from two-dimensional 1H nuclear magnetic resonance data. The structure features all the characteristics of the "cysteine-stabilized alpha beta-motif." A comparison of the structure, the electrostatic potential surface and regions important for interaction with the fungal receptor, is made with Rs-AFP1 (plant defensin of subfamily A3). Thus, residues important for activity and specificity have been assigned.

Selected figure(s)



	Figure 5. Figure 5. Polypeptide backbone of the Gln8-Asn16 fragment and the side chain of Trp10 of Ah-AMP1.		Figure 7. Figure 7. Schematic representation of the N- and C-termini and the disulfide bond connecting them for Ah-AMP1 (red) and Rs-AFP1 (green). The free electron pairs of the cysteine sulfur atoms are shown only for Rs-AFP1.

Figures were selected by an automated process.

Literature references that cite this PDB file's key reference

PubMed id

Reference

19533758

Y.F.Yang, K.C.Cheng, P.H.Tsai, C.C.Liu, T.R.Lee, and P.C.Lyu (2009).
Alanine substitutions of noncysteine residues in the cysteine-stabilized alphabeta motif.

Protein Sci, 18, 1498-1506.

16544327

Y.J.Liu, C.S.Cheng, S.M.Lai, M.P.Hsu, C.S.Chen, and P.C.Lyu (2006).
Solution structure of the plant defensin VrD1 from mung bean and its possible role in insecticidal activity against bruchids.

Proteins, 63, 777-786.

PDB code:

1ti5

15159575

X.Song, Z.Zhou, J.Wang, F.Wu, and W.Gong (2004).
Purification, characterization and preliminary crystallographic studies of a novel plant defensin from Pachyrrhizus erosus seeds.

Acta Crystallogr D Biol Crystallogr, 60, 1121-1124.

11856345

N.Mandard, P.Bulet, A.Caille, S.Daffre, and F.Vovelle (2002).
The solution structure of gomesin, an antimicrobial cysteine-rich peptide from the spider.

Eur J Biochem, 269, 1190-1198.

PDB code:

1kfp

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.