7zot

From Proteopedia

(Difference between revisions)

Current revision

crystal structure of PLAAT4 N-terminal domain

Structural highlights

7zot is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.735Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PLAT4_HUMAN Exhibits both phospholipase A1/2 and acyltransferase activities (PubMed:19615464, PubMed:22605381, PubMed:22825852, PubMed:26503625). Shows phospholipase A1 (PLA1) and A2 (PLA2), catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids (PubMed:19615464, PubMed:22605381, PubMed:22825852). For most substrates, PLA1 activity is much higher than PLA2 activity (PubMed:19615464). Shows O-acyltransferase activity, catalyzing the transfer of a fatty acyl group from glycerophospholipid to the hydroxyl group of lysophospholipid (PubMed:19615464). Shows N-acyltransferase activity, catalyzing the calcium-independent transfer of a fatty acyl group at the sn-1 position of phosphatidylcholine (PC) and other glycerophospholipids to the primary amine of phosphatidylethanolamine (PE), forming N-acylphosphatidylethanolamine (NAPE), which serves as precursor for N-acylethanolamines (NAEs) (PubMed:19615464, PubMed:22605381, PubMed:22825852). Promotes keratinocyte differentiation via activation of TGM1 (PubMed:17762858).^[1] ^[2] ^[3] ^[4] ^[5]

Publication Abstract from PubMed

Phospholipase A and Acyltransferase 4 (PLAAT4) is a class II tumor suppressor, that also plays a role as a restrictor of intracellular Toxoplasma gondii infection through restriction of parasitic vacuole size. The catalytic N-terminal domain (NTD) interacts with the C-terminal domain (CTD), which is important for sub-cellular targeting and enzymatic function. The dynamics of the NTD main (L1) loop and the L2(B6) loop adjacent to the active site, have been shown to be important regulators of enzymatic activity. Here, we present the crystal structure of PLAAT4 NTD, determined from severely intergrown crystals using automated, laser-based crystal harvesting and data reduction technologies. The structure showed the L1 loop in two distinct conformations, highlighting a complex network of interactions likely influencing its conformational flexibility. Ensemble refinement of the crystal structure recapitulates the major correlated motions observed in solution by NMR. Our analysis offers useful insights on millisecond dynamics based on the crystal structure, complementing NMR studies which preclude structural information at this time scale.

Crystal structure of the phospholipase A and acyltransferase 4 (PLAAT4) catalytic domain.,Wehlin A, Cornaciu I, Marquez JA, Perrakis A, von Castelmur E J Struct Biol. 2022 Oct 7;214(4):107903. doi: 10.1016/j.jsb.2022.107903. PMID:36210037^[6]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Jans R, Sturniolo MT, Eckert RL. Localization of the TIG3 transglutaminase interaction domain and demonstration that the amino-terminal region is required for TIG3 function as a keratinocyte differentiation regulator. J Invest Dermatol. 2008 Mar;128(3):517-29. doi: 10.1038/sj.jid.5701035. Epub 2007, Aug 30. PMID:17762858 doi:http://dx.doi.org/10.1038/sj.jid.5701035
↑ Uyama T, Jin XH, Tsuboi K, Tonai T, Ueda N. Characterization of the human tumor suppressors TIG3 and HRASLS2 as phospholipid-metabolizing enzymes. Biochim Biophys Acta. 2009 Dec;1791(12):1114-24. doi:, 10.1016/j.bbalip.2009.07.001. Epub 2009 Jul 14. PMID:19615464 doi:http://dx.doi.org/10.1016/j.bbalip.2009.07.001
↑ Golczak M, Kiser PD, Sears AE, Lodowski DT, Blaner WS, Palczewski K. Structural Basis for the Acyltransferase Activity of Lecithin:Retinol Acyltransferase-like Proteins. J Biol Chem. 2012 Jul 6;287(28):23790-807. Epub 2012 May 17. PMID:22605381 doi:10.1074/jbc.M112.361550
↑ Uyama T, Ikematsu N, Inoue M, Shinohara N, Jin XH, Tsuboi K, Tonai T, Tokumura A, Ueda N. Generation of N-acylphosphatidylethanolamine by members of the phospholipase A/acyltransferase (PLA/AT) family. J Biol Chem. 2012 Sep 14;287(38):31905-19. doi: 10.1074/jbc.M112.368712. Epub, 2012 Jul 23. PMID:22825852 doi:http://dx.doi.org/10.1074/jbc.M112.368712
↑ Mardian EB, Bradley RM, Duncan RE. The HRASLS (PLA/AT) subfamily of enzymes. J Biomed Sci. 2015 Oct 26;22:99. doi: 10.1186/s12929-015-0210-7. PMID:26503625 doi:http://dx.doi.org/10.1186/s12929-015-0210-7
↑ Wehlin A, Cornaciu I, Marquez JA, Perrakis A, von Castelmur E. Crystal structure of the phospholipase A and acyltransferase 4 (PLAAT4) catalytic domain. J Struct Biol. 2022 Oct 7;214(4):107903. doi: 10.1016/j.jsb.2022.107903. PMID:36210037 doi:http://dx.doi.org/10.1016/j.jsb.2022.107903

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/7zot"

Categories: Homo sapiens | Large Structures | Cornaciu I | Perrakis A | Von Castelmur E

@@ Line 4: / Line 4: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[7zot]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ZOT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ZOT FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.735&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></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=7zot FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7zot OCA], [https://pdbe.org/7zot PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7zot RCSB], [https://www.ebi.ac.uk/pdbsum/7zot PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7zot ProSAT]</span></td></tr>
 </table>

7zot

From Proteopedia

Current revision

crystal structure of PLAAT4 N-terminal domain

Structural highlights

Function

Publication Abstract from PubMed

References

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