1oxw

<table><tr><td colspan='2'>[[1oxw]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Heartleaf_nightshade Heartleaf nightshade]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OXW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OXW FirstGlance]. <br>

</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>

<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=1oxw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oxw OCA], [http://pdbe.org/1oxw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1oxw RCSB], [http://www.ebi.ac.uk/pdbsum/1oxw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1oxw ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Patatin is a nonspecific lipid acyl hydrolase that accounts for approximately 40% of the total soluble protein in mature potato tubers, and it has potent insecticidal activity against the corn rootworm. We determined the X-ray crystal structure of a His-tagged variant of an isozyme of patatin, Pat17, to 2.2 A resolution, employing SeMet multiwavelength anomalous dispersion (MAD) phasing methods. The patatin crystal structure has three molecules in the asymmetric unit, an R-factor of 22.0%, and an R(free) of 27.2% (for 10% of the data not included in the refinement) and includes 498 water molecules. The structure notably revealed that patatin has a Ser-Asp catalytic dyad and an active site like that of human cytosolic phospholipase A(2) (cPLA(2)) [Dessen, A., et al. (1999) Cell 97, 349-360]. In addition, patatin has a folding topology related to that of the catalytic domain of cPLA(2) and unlike the canonical alpha/beta-hydrolase fold. The structure confirms our site-directed mutagenesis and bioactivity data that initially suggested patatin possessed a Ser-Asp catalytic dyad. Alanine-scanning mutagenesis revealed that Ser77 and Asp215 were critical for both esterase and bioactivity, consistent with prior work implicating a Ser residue [Strickland, J. H., et al. (1995) Plant Physiol. 109, 667-674] and a Ser-Asp dyad [Hirschberg, H. J. H. B., et al. (2001) Eur. J. Biochem. 268, 5037-5044] in patatin's catalytic activity. The crystal structure aids the understanding of other structure-function relationships in patatin. Patatin does not display interfacial activation, a hallmark feature of lipases, and this is likely due to the fact that it lacks a flexible lid that can shield the active site.

The crystal structure, mutagenesis, and activity studies reveal that patatin is a lipid acyl hydrolase with a Ser-Asp catalytic dyad.,Rydel TJ, Williams JM, Krieger E, Moshiri F, Stallings WC, Brown SM, Pershing JC, Purcell JP, Alibhai MF Biochemistry. 2003 Jun 10;42(22):6696-708. PMID:12779324<ref>PMID:12779324</ref>

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

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== References ==

<references/>

[[Category: Heartleaf nightshade]]

[[Category: Alibhai, M F]]

[[Category: Brown, S M]]

[[Category: Krieger, E]]

[[Category: Moshiri, F]]

[[Category: Pershing, J C]]

[[Category: Purcell, J P]]

[[Category: Rydel, T J]]

[[Category: Stallings, W C]]

[[Category: Williams, J M]]

[[Category: Plant protein]]