4fpr

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==Structure of a fungal protein==
==Structure of a fungal protein==
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<StructureSection load='4fpr' size='340' side='right' caption='[[4fpr]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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<StructureSection load='4fpr' size='340' side='right'caption='[[4fpr]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4fpr]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Blackleg_fungus Blackleg fungus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FPR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FPR FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4fpr]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Blackleg_fungus Blackleg fungus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FPR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FPR FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4fpq|4fpq]]</td></tr>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4fpq|4fpq]]</div></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AvrLm4-7, LEMA_P086290.1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=985895 Blackleg fungus])</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AvrLm4-7, LEMA_P086290.1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=985895 Blackleg fungus])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4fpr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fpr OCA], [http://pdbe.org/4fpr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fpr RCSB], [http://www.ebi.ac.uk/pdbsum/4fpr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fpr ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4fpr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fpr OCA], [https://pdbe.org/4fpr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fpr RCSB], [https://www.ebi.ac.uk/pdbsum/4fpr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fpr ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The avirulence gene AvrLm4-7 of Leptosphaeria maculans, the causal agent of stem canker in Brassica napus (oilseed rape), confers a dual specificity of recognition by two resistance genes (Rlm4 and Rlm7) and is strongly involved in fungal fitness. In order to elucidate the biological function of AvrLm4-7 and understand the specificity of recognition by Rlm4 and Rlm7, the AvrLm4-7 protein was produced in Pichia pastoris and its crystal structure was determined. It revealed the presence of four disulfide bridges, but no close structural analogs could be identified. A short stretch of amino acids in the C terminus of the protein, (R/N)(Y/F)(R/S)E(F/W), was well-conserved among AvrLm4-7 homologs. Loss of recognition of AvrLm4-7 by Rlm4 is caused by the mutation of a single glycine to an arginine residue located in a loop of the protein. Loss of recognition by Rlm7 is governed by more complex mutational patterns, including gene loss or drastic modifications of the protein structure. Three point mutations altered residues in the well-conserved C-terminal motif or close to the glycine involved in Rlm4-mediated recognition, resulting in the loss of Rlm7-mediated recognition. Transient expression in Nicotiana benthamiana (tobacco) and particle bombardment experiments on leaves from oilseed rape suggested that AvrLm4-7 interacts with its cognate R proteins inside the plant cell, and can be translocated into plant cells in the absence of the pathogen. Translocation of AvrLm4-7 into oilseed rape leaves is likely to require the (R/N)(Y/F)(R/S)E(F/W) motif as well as an RAWG motif located in a nearby loop that together form a positively charged region.
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Crystal structure of the effector AvrLm4-7 of Leptosphaeria maculans reveals insights into its translocation into plant cells and recognition by resistance proteins.,Blondeau K, Blaise F, Graille M, Kale SD, Linglin J, Ollivier B, Labarde A, Lazar N, Daverdin G, Balesdent MH, Choi DH, Tyler BM, Rouxel T, van Tilbeurgh H, Fudal I Plant J. 2015 Aug;83(4):610-24. doi: 10.1111/tpj.12913. Epub 2015 Jul 14. PMID:26082394<ref>PMID:26082394</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4fpr" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
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*[[Avirulence protein|Avirulence protein]]
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*[[Avirulence protein 3D structures|Avirulence protein 3D structures]]
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Blackleg fungus]]
[[Category: Blackleg fungus]]
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[[Category: Large Structures]]
[[Category: Balesdent, M H]]
[[Category: Balesdent, M H]]
[[Category: Blaise, F]]
[[Category: Blaise, F]]

Revision as of 04:56, 3 August 2022

Structure of a fungal protein

PDB ID 4fpr

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