2kyt

From Proteopedia

(Difference between revisions)

Revision as of 08:09, 18 January 2023

Solution structure of the H-REV107 N-terminal domain

Structural highlights

2kyt is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PLAT3_HUMAN Exhibits both phospholipase A1/2 and acyltransferase activities (PubMed:19615464, PubMed:19047760, PubMed:22825852, PubMed:22605381, PubMed:26503625). Shows phospholipase A1 (PLA1) and A2 (PLA2) activity, catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids (PubMed:19615464, PubMed:19047760, PubMed:22825852, PubMed:22605381, PubMed:22923616). 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:19047760, PubMed:22825852, PubMed:22605381). Exhibits high N-acyltransferase activity and low phospholipase A1/2 activity (PubMed:22825852). Required for complete organelle rupture and degradation that occur during eye lens terminal differentiation, when fiber cells that compose the lens degrade all membrane-bound organelles in order to provide lens with transparency to allow the passage of light. Organelle membrane degradation is probably catalyzed by the phospholipase activity (By similarity).[UniProtKB:Q8R3U1]^[1] ^[2] ^[3] ^[4] ^[5] ^[6] (Microbial infection) Acts as a host factor for picornaviruses: required during early infection to promote viral genome release into the cytoplasm (PubMed:28077878). May act as a cellular sensor of membrane damage at sites of virus entry, which relocalizes to sites of membrane rupture upon virus unfection (PubMed:28077878). Facilitates safe passage of the RNA away from LGALS8, enabling viral genome translation by host ribosome (PubMed:28077878). May also be involved in initiating pore formation, increasing pore size or in maintaining pores for genome delivery (PubMed:28077878). The lipid-modifying enzyme activity is required for this process (PubMed:28077878).^[7]

Publication Abstract from PubMed

H-REV107 is a Ca(2+)-independent phospholipase A(1/2), and it is also a pro-apoptosis protein belonging to the novel class II tumor suppressor family, H-REV107-like family. Here we report the solution structure of the N-terminal catalytic domain of human H-REV107, which has a similar architecture to classical NlpC/P60 domains, even though their fold topologies are different due to circular permutation in the primary sequence. The phospholipase active site possesses a structurally conserved Cys-His-His catalytic triad as found in NlpC/P60 peptidases, indicating H-REV107 should adopt a similar catalytic mechanism towards phospholipid substrates to that of NlpC/P60 peptidases towards peptides. As H-REV107 is highly similar to lecithin retinol acyltransferase, our study also provides structural insight to this essential enzyme in retinol metabolism.

Solution structure of the N-terminal catalytic domain of human H-REV107--a novel circular permutated NlpC/P60 domain.,Ren X, Lin J, Jin C, Xia B FEBS Lett. 2010 Oct 8;584(19):4222-6. Epub 2010 Sep 17. PMID:20837014^[8]

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

References

↑ Uyama T, Morishita J, Jin XH, Okamoto Y, Tsuboi K, Ueda N. The tumor suppressor gene H-Rev107 functions as a novel Ca2+-independent cytosolic phospholipase A1/2 of the thiol hydrolase type. J Lipid Res. 2009 Apr;50(4):685-93. doi: 10.1194/jlr.M800453-JLR200. Epub 2008, Dec 1. PMID:19047760 doi:http://dx.doi.org/10.1194/jlr.M800453-JLR200
↑ 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
↑ Pang XY, Cao J, Addington L, Lovell S, Battaile KP, Zhang N, Rao JL, Dennis EA, Moise AR. Structure/Function Relationships of Adipose Phospholipase A2 Containing a Cys-His-His Catalytic Triad. J Biol Chem. 2012 Aug 25. PMID:22923616 doi:http://dx.doi.org/10.1074/jbc.M112.398859
↑ 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
↑ Staring J, von Castelmur E, Blomen VA, van den Hengel LG, Brockmann M, Baggen J, Thibaut HJ, Nieuwenhuis J, Janssen H, van Kuppeveld FJ, Perrakis A, Carette JE, Brummelkamp TR. PLA2G16 represents a switch between entry and clearance of Picornaviridae. Nature. 2017 Jan 19;541(7637):412-416. doi: 10.1038/nature21032. Epub 2017 Jan, 11. PMID:28077878 doi:http://dx.doi.org/10.1038/nature21032
↑ Ren X, Lin J, Jin C, Xia B. Solution structure of the N-terminal catalytic domain of human H-REV107--a novel circular permutated NlpC/P60 domain. FEBS Lett. 2010 Oct 8;584(19):4222-6. Epub 2010 Sep 17. PMID:20837014 doi:10.1016/j.febslet.2010.09.015

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2kyt"

Categories: Homo sapiens | Large Structures | Ren X | Xia B

@@ Line 1: / Line 1: @@
 ==Solution structure of the H-REV107 N-terminal domain==
-<StructureSection load='2kyt' size='340' side='right'caption='[[2kyt]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2kyt' size='340' side='right'caption='[[2kyt]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2kyt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KYT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KYT FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2kyt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KYT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KYT FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PLA2G16, HRASLS3, HREV107 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+</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=2kyt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kyt OCA], [https://pdbe.org/2kyt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kyt RCSB], [https://www.ebi.ac.uk/pdbsum/2kyt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kyt ProSAT]</span></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Phospholipase_A(2) Phospholipase A(2)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.4 3.1.1.4] </span></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=2kyt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kyt OCA], [https://pdbe.org/2kyt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kyt RCSB], [https://www.ebi.ac.uk/pdbsum/2kyt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kyt ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/HRSL3_HUMAN HRSL3_HUMAN]] Exhibits PLA1/2 activity, catalyzing the calcium-independent hydrolysis of acyl groups in various phosphatidylcholines (PC) and phosphatidylethanolamine (PE). For most substrates, PLA1 activity is much higher than PLA2 activity. Specifically catalyzes the release of fatty acids from phospholipids in adipose tissue (By similarity). N- and O-acylation activity is hardly detectable. Might decrease protein phosphatase 2A (PP2A) activity.<ref>PMID:17374643</ref> <ref>PMID:19615464</ref>
+[https://www.uniprot.org/uniprot/PLAT3_HUMAN PLAT3_HUMAN] Exhibits both phospholipase A1/2 and acyltransferase activities (PubMed:19615464, PubMed:19047760, PubMed:22825852, PubMed:22605381, PubMed:26503625). Shows phospholipase A1 (PLA1) and A2 (PLA2) activity, catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids (PubMed:19615464, PubMed:19047760, PubMed:22825852, PubMed:22605381, PubMed:22923616). 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:19047760, PubMed:22825852, PubMed:22605381). Exhibits high N-acyltransferase activity and low phospholipase A1/2 activity (PubMed:22825852). Required for complete organelle rupture and degradation that occur during eye lens terminal differentiation, when fiber cells that compose the lens degrade all membrane-bound organelles in order to provide lens with transparency to allow the passage of light. Organelle membrane degradation is probably catalyzed by the phospholipase activity (By similarity).[UniProtKB:Q8R3U1]<ref>PMID:19047760</ref> <ref>PMID:19615464</ref> <ref>PMID:22605381</ref> <ref>PMID:22825852</ref> <ref>PMID:22923616</ref> <ref>PMID:26503625</ref>   (Microbial infection) Acts as a host factor for picornaviruses: required during early infection to promote viral genome release into the cytoplasm (PubMed:28077878). May act as a cellular sensor of membrane damage at sites of virus entry, which relocalizes to sites of membrane rupture upon virus unfection (PubMed:28077878). Facilitates safe passage of the RNA away from LGALS8, enabling viral genome translation by host ribosome (PubMed:28077878). May also be involved in initiating pore formation, increasing pore size or in maintaining pores for genome delivery (PubMed:28077878). The lipid-modifying enzyme activity is required for this process (PubMed:28077878).<ref>PMID:28077878</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 26: / Line 24: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Ren, X]]
+[[Category: Ren X]]
-[[Category: Xia, B]]
+[[Category: Xia B]]
-[[Category: H-rev107]]
-[[Category: Hydrolase]]
-[[Category: N-terminal domain]]
-[[Category: Phospholipase]]
-[[Category: Tumor suppressor]]

2kyt

From Proteopedia

Revision as of 08:09, 18 January 2023

Solution structure of the H-REV107 N-terminal domain

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

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