View source for 1kg1


==NMR structure of the NIP1 elicitor protein from Rhynchosporium secalis==
<StructureSection load='1kg1' size='340' side='right'caption='[[1kg1]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1kg1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhynchosporium_secalis Rhynchosporium secalis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KG1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KG1 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kg1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kg1 OCA], [https://pdbe.org/1kg1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kg1 RCSB], [https://www.ebi.ac.uk/pdbsum/1kg1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kg1 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q02039_RHYSE Q02039_RHYSE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Activation of the disease resistance response in a host plant frequently requires the interaction of a plant resistance gene product with a corresponding, pathogenderived signal encoded by an avirulence gene. The products of resistance genes from diverse plant species show remarkable structural similarity. However, due to the general paucity of information on pathogen avirulence genes the recognition process remains in most cases poorly understood. NIP1, a small protein secreted by the fungal barley pathogen Rhynchosporium secalis, is one of only a few fungal avirulence proteins identified and characterized to date. The defense-activating activity of NIP1 is mediated by barley resistance gene Rrs1. In addition, a role of the protein in fungal virulence is suggested by its nonspecific toxicity in leaf tissues of host and non-host cereals as well as its resistance gene-independent stimulatory effect on the plant plasma membrane H+-ATPase. Four naturally occurring NIP1 isoforms are characterized by single amino acid alterations that affect the different activities in a similar way. As a step toward unraveling the signal perception/transduction mechanism, the solution structure of NIP1 was determined. The protein structure is characterized by a novel fold. It consists of two parts containing beta-sheets of two and three anti-parallel strands, respectively. Five intramolecular disulfide bonds, comprising a novel disulfide bond pattern, stabilize these parts and their position with respect to each other. A comparative analysis of the protein structure with the properties of the NIP1 isoforms suggests two loop regions to be crucial for the resistance-triggering activity of NIP1.

Solution structure of the plant disease resistance-triggering protein NIP1 from the fungus Rhynchosporium secalis shows a novel beta-sheet fold.,van't Slot KA, van den Burg HA, Kloks CP, Hilbers CW, Knogge W, Papavoine CH J Biol Chem. 2003 Nov 14;278(46):45730-6. Epub 2003 Aug 27. PMID:12944393<ref>PMID:12944393</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1kg1" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rhynchosporium secalis]]
[[Category: Hilbers CW]]
[[Category: Kloks CP]]
[[Category: Knogge W]]
[[Category: Papavoine CH]]
[[Category: Van den Burg HA]]
[[Category: Van't Slot KA]]