PDBsum entry 6sgo

Unknown function

PDB id: 6sgo

Contents

Protein chain

136 a.a.

PDB id:

6sgo

Name:

Unknown function

Title:

Nmr structure of mlp124017

Structure:

Secreted protein. Chain: a. Synonym: mlp124017. Engineered: yes

Source:

Melampsora larici-populina. Poplar leaf rust fungus. Organism_taxid: 203908. Strain: 98ag31 / pathotype 3-4-7. Gene: melladraft_124017. Expressed in: escherichia coli. Expression_system_taxid: 562

NMR struc:

20 models

Authors:

P.Barthe,K.De Guillen,A.Padilla,A.Hecker

Key ref:

K.de Guillen et al. (2019). Structural genomics applied to the rust fungus Melampsora larici-populina reveals two candidate effector proteins adopting cystine knot and NTF2-like protein folds. Sci Rep, 9, 18084. PubMed id: 31792250 DOI: 10.1038/s41598-019-53816-9

Date:

05-Aug-19 Release date: 18-Dec-19

Protein chain

F4S7L2  (F4S7L2_MELLP) -  Secreted protein from Melampsora larici-populina (strain 98AG31 / pathotype 3-4-7)

Seq: 165 a.a.

Struc: 136 a.a.*

* PDB and UniProt seqs differ at 14 residue positions (black crosses)

DOI no: 10.1038/s41598-019-53816-9

Sci Rep 9:18084 (2019)

PubMed id: 31792250

Structural genomics applied to the rust fungus Melampsora larici-populina reveals two candidate effector proteins adopting cystine knot and NTF2-like protein folds.

K.de Guillen, C.Lorrain, P.Tsan, P.Barthe, B.Petre, N.Saveleva, N.Rouhier, S.Duplessis, A.Padilla, A.Hecker.

ABSTRACT

Rust fungi are plant pathogens that secrete an arsenal of effector proteins interfering with plant functions and promoting parasitic infection. Effectors are often species-specific, evolve rapidly, and display low sequence similarities with known proteins. How rust fungal effectors function in host cells remains elusive, and biochemical and structural approaches have been scarcely used to tackle this question. In this study, we produced recombinant proteins of eleven candidate effectors of the leaf rust fungus Melampsora larici-populina in Escherichia coli. We successfully purified and solved the three-dimensional structure of two proteins, MLP124266 and MLP124017, using NMR spectroscopy. Although both MLP124266 and MLP124017 show no sequence similarity with known proteins, they exhibit structural similarities to knottins, which are disulfide-rich small proteins characterized by intricate disulfide bridges, and to nuclear transport factor 2-like proteins, which are molecular containers involved in a wide range of functions, respectively. Interestingly, such structural folds have not been reported so far in pathogen effectors, indicating that MLP124266 and MLP124017 may bear novel functions related to pathogenicity. Our findings show that sequence-unrelated effectors can adopt folds similar to known proteins, and encourage the use of biochemical and structural approaches to functionally characterize effector candidates.