1nh1

<table><tr><td colspan='2'>[[1nh1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_19310 Atcc 19310]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NH1 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1NH1 FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AVRB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=317 ATCC 19310])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1nh1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nh1 OCA], [http://pdbe.org/1nh1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1nh1 RCSB], [http://www.ebi.ac.uk/pdbsum/1nh1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1nh1 ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

AvrB is a Pseudomonas syringae type III effector protein that is translocated into host plant cells during attempted pathogenesis. Arabidopsis harboring the corresponding resistance protein RPM1 can detect AvrB and mount a rapid host defense response, thus avoiding active infection. In the plant cell, AvrB induces phosphorylation of RIN4, a key component in AvrB/RPM1 recognition. Although the AvrB/RPM1 system is among the best characterized of the numerous bacterial effector/plant resistance protein systems involved in plant disease resistance and pathogenesis, the details of the molecular recognition mechanism are still unclear. To gain further insights, the crystal structure of AvrB was determined. The 2.2 A structure exhibits a novel mixed alpha/beta bilobal fold. Aided by the structural information, we demonstrate that one lobe is the determinant of AvrB/RPM1 recognition specificity. This structural information and preliminary structure-function studies provide a framework for the future understanding of AvrB function on the molecular level.

Crystal structure of the type III effector AvrB from Pseudomonas syringae.,Lee CC, Wood MD, Ng K, Andersen CB, Liu Y, Luginbuhl P, Spraggon G, Katagiri F Structure. 2004 Mar;12(3):487-94. PMID:15016364<ref>PMID:15016364</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Atcc 19310]]

[[Category: Katagiri, F]]

[[Category: Lee, C C]]

[[Category: Luginbuhl, P]]

[[Category: Ng, K]]

[[Category: Spraggon, G]]

[[Category: Wood, M D]]

[[Category: Helix bundle]]