2kte

<StructureSection load='2kte' size='340' side='right'caption='[[2kte]], [[NMR_Ensembles_of_Models | 18 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[2kte]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KTE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KTE FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">yndB, BSU17730 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835])</td></tr>

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== Publication Abstract from PubMed ==

The solution structure of the Bacillus subtilis protein YndB has been solved using NMR to investigate proposed biological functions. The YndB structure exhibits the helix-grip fold, which consists of a beta-sheet with two small and one long alpha-helix, forming a hydrophobic cavity that preferentially binds lipid-like molecules. Sequence and structure comparisons with proteins from eukaryotes, prokaryotes, and archaea suggest that YndB is very similar to the eukaryote protein Aha1, which binds to the middle domain of Hsp90 and induces ATPase activity. On the basis of these similarities, YndB has been classified as a member of the activator of Hsp90 ATPase homolog 1-like protein (AHSA1) family with a function that appears to be related to stress response. An in silico screen of a compound library of approximately 18,500 lipids was used to identify classes of lipids that preferentially bind YndB. The in silico screen identified, in order of affinity, the chalcone/hydroxychalcone, flavanone, and flavone/flavonol classes of lipids, which was further verified by 2D (1) H-(15) N HSQC NMR titration experiments with trans-chalcone, flavanone, flavone, and flavonol. All of these compounds are typically found in plants as precursors to various flavonoid antibiotics and signaling molecules. The sum of the data suggests an involvement of YndB with the stress response of B. subtilis to chalcone-like flavonoids released by plants due to a pathogen infection. The observed binding of chalcone-like molecules by YndB is likely related to the symbiotic relationship between B. subtilis and plants.

Solution structure and function of YndB, an AHSA1 protein from Bacillus subtilis.,Stark JL, Mercier KA, Mueller GA, Acton TB, Xiao R, Montelione GT, Powers R Proteins. 2010 Dec;78(16):3328-40. doi: 10.1002/prot.22840. PMID:20818668<ref>PMID:20818668</ref>

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

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<div class="pdbe-citations 2kte" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Vibrio subtilis ehrenberg 1835]]

[[Category: Acton, T B]]

[[Category: Ciano, M]]

[[Category: Ho, C]]

[[Category: Lui, J]]

[[Category: Ma, L]]

[[Category: Mercier, K A]]

[[Category: Montelione, G T]]

[[Category: Mueller, G A]]

[[Category: Structural genomic]]

[[Category: Powers, R]]

[[Category: Rossi, R]]

[[Category: Rost, B]]

[[Category: Xiao, R]]

[[Category: Unknown function]]