6wq1

From Proteopedia

(Difference between revisions)

Current revision

Eukaryotic LanCL2 protein

Structural highlights

6wq1 is a 4 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 2.295Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LANC2_HUMAN Necessary for abscisic acid (ABA) binding on the cell membrane and activation of the ABA signaling pathway in granulocytes.^[1]

Publication Abstract from PubMed

Enzyme-mediated damage repair or mitigation, while common for nucleic acids, is rare for proteins. Examples of protein damage are elimination of phosphorylated Ser/Thr to dehydroalanine/dehydrobutyrine (Dha/Dhb) in pathogenesis and aging. Bacterial LanC enzymes use Dha/Dhb to form carbon-sulfur linkages in antimicrobial peptides, but the functions of eukaryotic LanC-like (LanCL) counterparts are unknown. We show that LanCLs catalyze the addition of glutathione to Dha/Dhb in proteins, driving irreversible C-glutathionylation. Chemo-enzymatic methods were developed to site-selectively incorporate Dha/Dhb at phospho-regulated sites in kinases. In human MAPK-MEK1, such "elimination damage" generated aberrantly activated kinases, which were deactivated by LanCL-mediated C-glutathionylation. Surveys of endogenous proteins bearing damage from elimination (the eliminylome) also suggest it is a source of electrophilic reactivity. LanCLs thus remove these reactive electrophiles and their potentially dysregulatory effects from the proteome. As knockout of LanCL in mice can result in premature death, repair of this kind of protein damage appears important physiologically.

LanCLs add glutathione to dehydroamino acids generated at phosphorylated sites in the proteome.,Lai KY, Galan SRG, Zeng Y, Zhou TH, He C, Raj R, Riedl J, Liu S, Chooi KP, Garg N, Zeng M, Jones LH, Hutchings GJ, Mohammed S, Nair SK, Chen J, Davis BG, van der Donk WA Cell. 2021 May 13;184(10):2680-2695.e26. doi: 10.1016/j.cell.2021.04.001. Epub, 2021 Apr 30. PMID:33932340^[2]

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

References

↑ Sturla L, Fresia C, Guida L, Bruzzone S, Scarfi S, Usai C, Fruscione F, Magnone M, Millo E, Basile G, Grozio A, Jacchetti E, Allegretti M, De Flora A, Zocchi E. LANCL2 is necessary for abscisic acid binding and signaling in human granulocytes and in rat insulinoma cells. J Biol Chem. 2009 Oct 9;284(41):28045-28057. doi: 10.1074/jbc.M109.035329. Epub, 2009 Aug 10. PMID:19667068 doi:http://dx.doi.org/10.1074/jbc.M109.035329
↑ Lai KY, Galan SRG, Zeng Y, Zhou TH, He C, Raj R, Riedl J, Liu S, Chooi KP, Garg N, Zeng M, Jones LH, Hutchings GJ, Mohammed S, Nair SK, Chen J, Davis BG, van der Donk WA. LanCLs add glutathione to dehydroamino acids generated at phosphorylated sites in the proteome. Cell. 2021 May 13;184(10):2680-2695.e26. doi: 10.1016/j.cell.2021.04.001. Epub, 2021 Apr 30. PMID:33932340 doi:http://dx.doi.org/10.1016/j.cell.2021.04.001

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/6wq1"

Categories: Homo sapiens | Large Structures | Garg N | Nair SK

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6wq1 is ON HOLD  until Paper Publication
+==Eukaryotic LanCL2 protein==
+<StructureSection load='6wq1' size='340' side='right'caption='[[6wq1]], [[Resolution|resolution]] 2.29&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6wq1]] is a 4 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=6WQ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6WQ1 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.295&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=6wq1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wq1 OCA], [https://pdbe.org/6wq1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6wq1 RCSB], [https://www.ebi.ac.uk/pdbsum/6wq1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6wq1 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/LANC2_HUMAN LANC2_HUMAN] Necessary for abscisic acid (ABA) binding on the cell membrane and activation of the ABA signaling pathway in granulocytes.<ref>PMID:19667068</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Enzyme-mediated damage repair or mitigation, while common for nucleic acids, is rare for proteins. Examples of protein damage are elimination of phosphorylated Ser/Thr to dehydroalanine/dehydrobutyrine (Dha/Dhb) in pathogenesis and aging. Bacterial LanC enzymes use Dha/Dhb to form carbon-sulfur linkages in antimicrobial peptides, but the functions of eukaryotic LanC-like (LanCL) counterparts are unknown. We show that LanCLs catalyze the addition of glutathione to Dha/Dhb in proteins, driving irreversible C-glutathionylation. Chemo-enzymatic methods were developed to site-selectively incorporate Dha/Dhb at phospho-regulated sites in kinases. In human MAPK-MEK1, such "elimination damage" generated aberrantly activated kinases, which were deactivated by LanCL-mediated C-glutathionylation. Surveys of endogenous proteins bearing damage from elimination (the eliminylome) also suggest it is a source of electrophilic reactivity. LanCLs thus remove these reactive electrophiles and their potentially dysregulatory effects from the proteome. As knockout of LanCL in mice can result in premature death, repair of this kind of protein damage appears important physiologically.
-Authors: Nair, S.K., Garg, N.
+LanCLs add glutathione to dehydroamino acids generated at phosphorylated sites in the proteome.,Lai KY, Galan SRG, Zeng Y, Zhou TH, He C, Raj R, Riedl J, Liu S, Chooi KP, Garg N, Zeng M, Jones LH, Hutchings GJ, Mohammed S, Nair SK, Chen J, Davis BG, van der Donk WA Cell. 2021 May 13;184(10):2680-2695.e26. doi: 10.1016/j.cell.2021.04.001. Epub, 2021 Apr 30. PMID:33932340<ref>PMID:33932340</ref>
-Description: Eukaryotic LanCL2 protein
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Garg, N]]
+<div class="pdbe-citations 6wq1" style="background-color:#fffaf0;"></div>
-[[Category: Nair, S.K]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Garg N]]
+[[Category: Nair SK]]

6wq1

From Proteopedia

Current revision

Eukaryotic LanCL2 protein

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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