4r3z

From Proteopedia

(Difference between revisions)

Revision as of 06:39, 2 March 2023

Crystal structure of human ArgRS-GlnRS-AIMP1 complex

Structural highlights

4r3z is a 3 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

AIMP1_HUMAN Defects in AIMP1 are the cause of leukodystrophy hypomyelinating type 3 (HLD3) [MIM:260600. A severe autosomal recessive hypomyelinating leukodystrophy characterized by early infantile onset of global developmental delay, lack of development, lack of speech acquisition, and peripheral spasticity associated with decreased myelination in the central nervous system.^[1]

Function

AIMP1_HUMAN Non-catalytic component of the multisynthase complex. Stimulates the catalytic activity of cytoplasmic arginyl-tRNA synthase. Binds tRNA. Possesses inflammatory cytokine activity. Negatively regulates TGF-beta signaling through stabilization of SMURF2 by binding to SMURF2 and inhibiting its SMAD7-mediated degradation. Involved in glucose homeostasis through induction of glucagon secretion at low glucose levels. Promotes dermal fibroblast proliferation and wound repair. Regulates KDELR1-mediated retention of HSP90B1/gp96 in the endoplasmic reticulum. Plays a role in angiogenesis by inducing endothelial cell migration at low concentrations and endothelian cell apoptosis at high concentrations. Induces maturation of dendritic cells and monocyte cell adhesion. Modulates endothelial cell responses by degrading HIF-1A through interaction with PSMA7.^[2] ^[3] ^[4] ^[5] ^[6] ^[7]

Publication Abstract from PubMed

In higher eukaryotes, one of the two arginyl-tRNA synthetases (ArgRSs) has evolved to have an extended N-terminal domain that plays a crucial role in protein synthesis and cell growth and in integration into the multisynthetase complex (MSC). Here, we report a crystal structure of the MSC subcomplex comprising ArgRS, glutaminyl-tRNA synthetase (GlnRS), and the auxiliary factor aminoacyl tRNA synthetase complex-interacting multifunctional protein 1 (AIMP1)/p43. In this complex, the N-terminal domain of ArgRS forms a long coiled-coil structure with the N-terminal helix of AIMP1 and anchors the C-terminal core of GlnRS, thereby playing a central role in assembly of the three components. Mutation of AIMP1 destabilized the N-terminal helix of ArgRS and abrogated its catalytic activity. Mutation of the N-terminal helix of ArgRS liberated GlnRS, which is known to control cell death. This ternary complex was further anchored to AIMP2/p38 through interaction with AIMP1. These findings demonstrate the importance of interactions between the N-terminal domains of ArgRS and AIMP1 for the catalytic and noncatalytic activities of ArgRS and for the assembly of the higher-order MSC protein complex.

Structure of the ArgRS-GlnRS-AIMP1 complex and its implications for mammalian translation.,Fu Y, Kim Y, Jin KS, Kim HS, Kim JH, Wang D, Park M, Jo CH, Kwon NH, Kim D, Kim MH, Jeon YH, Hwang KY, Kim S, Cho Y Proc Natl Acad Sci U S A. 2014 Oct 21;111(42):15084-9. doi:, 10.1073/pnas.1408836111. Epub 2014 Oct 6. PMID:25288775^[8]

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

References

↑ Feinstein M, Markus B, Noyman I, Shalev H, Flusser H, Shelef I, Liani-Leibson K, Shorer Z, Cohen I, Khateeb S, Sivan S, Birk OS. Pelizaeus-Merzbacher-like disease caused by AIMP1/p43 homozygous mutation. Am J Hum Genet. 2010 Dec 10;87(6):820-8. doi: 10.1016/j.ajhg.2010.10.016. Epub, 2010 Nov 18. PMID:21092922 doi:10.1016/j.ajhg.2010.10.016
↑ Park SG, Jung KH, Lee JS, Jo YJ, Motegi H, Kim S, Shiba K. Precursor of pro-apoptotic cytokine modulates aminoacylation activity of tRNA synthetase. J Biol Chem. 1999 Jun 11;274(24):16673-6. PMID:10358004
↑ Shalak V, Kaminska M, Mitnacht-Kraus R, Vandenabeele P, Clauss M, Mirande M. The EMAPII cytokine is released from the mammalian multisynthetase complex after cleavage of its p43/proEMAPII component. J Biol Chem. 2001 Jun 29;276(26):23769-76. Epub 2001 Apr 16. PMID:11306575 doi:10.1074/jbc.M100489200
↑ Park SG, Kang YS, Ahn YH, Lee SH, Kim KR, Kim KW, Koh GY, Ko YG, Kim S. Dose-dependent biphasic activity of tRNA synthetase-associating factor, p43, in angiogenesis. J Biol Chem. 2002 Nov 22;277(47):45243-8. Epub 2002 Sep 16. PMID:12237313 doi:10.1074/jbc.M207934200
↑ Park H, Park SG, Lee JW, Kim T, Kim G, Ko YG, Kim S. Monocyte cell adhesion induced by a human aminoacyl-tRNA synthetase-associated factor, p43: identification of the related adhesion molecules and signal pathways. J Leukoc Biol. 2002 Feb;71(2):223-30. PMID:11818442
↑ Tandle AT, Calvani M, Uranchimeg B, Zahavi D, Melillo G, Libutti SK. Endothelial monocyte activating polypeptide-II modulates endothelial cell responses by degrading hypoxia-inducible factor-1alpha through interaction with PSMA7, a component of the proteasome. Exp Cell Res. 2009 Jul 1;315(11):1850-9. doi: 10.1016/j.yexcr.2009.03.021. Epub, 2009 Apr 10. PMID:19362550 doi:10.1016/j.yexcr.2009.03.021
↑ Renault L, Kerjan P, Pasqualato S, Menetrey J, Robinson JC, Kawaguchi S, Vassylyev DG, Yokoyama S, Mirande M, Cherfils J. Structure of the EMAPII domain of human aminoacyl-tRNA synthetase complex reveals evolutionary dimer mimicry. EMBO J. 2001 Feb 1;20(3):570-8. PMID:11157763 doi:10.1093/emboj/20.3.570
↑ Fu Y, Kim Y, Jin KS, Kim HS, Kim JH, Wang D, Park M, Jo CH, Kwon NH, Kim D, Kim MH, Jeon YH, Hwang KY, Kim S, Cho Y. Structure of the ArgRS-GlnRS-AIMP1 complex and its implications for mammalian translation. Proc Natl Acad Sci U S A. 2014 Oct 21;111(42):15084-9. doi:, 10.1073/pnas.1408836111. Epub 2014 Oct 6. PMID:25288775 doi:http://dx.doi.org/10.1073/pnas.1408836111

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4r3z"

Categories: Homo sapiens | Large Structures | Cho Y | Fu Y | Kim Y

@@ Line 3: / Line 3: @@
 <StructureSection load='4r3z' size='340' side='right'caption='[[4r3z]], [[Resolution|resolution]] 4.03&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4r3z]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R3Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R3Z FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4r3z]] is a 3 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=4R3Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4R3Z FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AIMP1, EMAP2, SCYE1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), RARS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), QARS ([http://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=4r3z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r3z OCA], [https://pdbe.org/4r3z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r3z RCSB], [https://www.ebi.ac.uk/pdbsum/4r3z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r3z ProSAT]</span></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Arginine--tRNA_ligase Arginine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.19 6.1.1.19] </span></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=4r3z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r3z OCA], [http://pdbe.org/4r3z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4r3z RCSB], [http://www.ebi.ac.uk/pdbsum/4r3z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4r3z ProSAT]</span></td></tr>
 </table>
 == Disease ==
-[[http://www.uniprot.org/uniprot/AIMP1_HUMAN AIMP1_HUMAN]] Defects in AIMP1 are the cause of leukodystrophy hypomyelinating type 3 (HLD3) [MIM:[http://omim.org/entry/260600 260600]]. A severe autosomal recessive hypomyelinating leukodystrophy characterized by early infantile onset of global developmental delay, lack of development, lack of speech acquisition, and peripheral spasticity associated with decreased myelination in the central nervous system.<ref>PMID:21092922</ref>  [[http://www.uniprot.org/uniprot/SYQ_HUMAN SYQ_HUMAN]] The disease is caused by mutations affecting the gene represented in this entry.
+[https://www.uniprot.org/uniprot/AIMP1_HUMAN AIMP1_HUMAN] Defects in AIMP1 are the cause of leukodystrophy hypomyelinating type 3 (HLD3) [MIM:[https://omim.org/entry/260600 260600]. A severe autosomal recessive hypomyelinating leukodystrophy characterized by early infantile onset of global developmental delay, lack of development, lack of speech acquisition, and peripheral spasticity associated with decreased myelination in the central nervous system.<ref>PMID:21092922</ref>
 == Function ==
-[[http://www.uniprot.org/uniprot/AIMP1_HUMAN AIMP1_HUMAN]] Non-catalytic component of the multisynthase complex. Stimulates the catalytic activity of cytoplasmic arginyl-tRNA synthase. Binds tRNA. Possesses inflammatory cytokine activity. Negatively regulates TGF-beta signaling through stabilization of SMURF2 by binding to SMURF2 and inhibiting its SMAD7-mediated degradation. Involved in glucose homeostasis through induction of glucagon secretion at low glucose levels. Promotes dermal fibroblast proliferation and wound repair. Regulates KDELR1-mediated retention of HSP90B1/gp96 in the endoplasmic reticulum. Plays a role in angiogenesis by inducing endothelial cell migration at low concentrations and endothelian cell apoptosis at high concentrations. Induces maturation of dendritic cells and monocyte cell adhesion. Modulates endothelial cell responses by degrading HIF-1A through interaction with PSMA7.<ref>PMID:10358004</ref> <ref>PMID:11306575</ref> <ref>PMID:12237313</ref> <ref>PMID:11818442</ref> <ref>PMID:19362550</ref> <ref>PMID:11157763</ref>  [[http://www.uniprot.org/uniprot/SYQ_HUMAN SYQ_HUMAN]] Plays a critical role in brain development.<ref>PMID:24656866</ref>  [[http://www.uniprot.org/uniprot/SYRC_HUMAN SYRC_HUMAN]] Forms part of a macromolecular complex that catalyzes the attachment of specific amino acids to cognate tRNAs during protein synthesis. Modulates the secretion of AIMP1 and may be involved in generation of the inflammatory cytokine EMAP2 from AIMP1.<ref>PMID:17443684</ref>
+[https://www.uniprot.org/uniprot/AIMP1_HUMAN AIMP1_HUMAN] Non-catalytic component of the multisynthase complex. Stimulates the catalytic activity of cytoplasmic arginyl-tRNA synthase. Binds tRNA. Possesses inflammatory cytokine activity. Negatively regulates TGF-beta signaling through stabilization of SMURF2 by binding to SMURF2 and inhibiting its SMAD7-mediated degradation. Involved in glucose homeostasis through induction of glucagon secretion at low glucose levels. Promotes dermal fibroblast proliferation and wound repair. Regulates KDELR1-mediated retention of HSP90B1/gp96 in the endoplasmic reticulum. Plays a role in angiogenesis by inducing endothelial cell migration at low concentrations and endothelian cell apoptosis at high concentrations. Induces maturation of dendritic cells and monocyte cell adhesion. Modulates endothelial cell responses by degrading HIF-1A through interaction with PSMA7.<ref>PMID:10358004</ref> <ref>PMID:11306575</ref> <ref>PMID:12237313</ref> <ref>PMID:11818442</ref> <ref>PMID:19362550</ref> <ref>PMID:11157763</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 25: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Arginine--tRNA ligase]]
+[[Category: Homo sapiens]]
-[[Category: Human]]
 [[Category: Large Structures]]
-[[Category: Cho, Y]]
+[[Category: Cho Y]]
-[[Category: Fu, Y]]
+[[Category: Fu Y]]
-[[Category: Kim, Y]]
+[[Category: Kim Y]]
-[[Category: Amino-acyl trna synthetase complex]]
-[[Category: Ligation amino acid to trna]]
-[[Category: Multi-synthetase complex]]
-[[Category: Protein binding-ligase complex]]

4r3z

From Proteopedia

Revision as of 06:39, 2 March 2023

Crystal structure of human ArgRS-GlnRS-AIMP1 complex

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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