4r3z

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<StructureSection load='4r3z' size='340' side='right'caption='[[4r3z]], [[Resolution|resolution]] 4.03&Aring;' scene=''>
<StructureSection load='4r3z' size='340' side='right'caption='[[4r3z]], [[Resolution|resolution]] 4.03&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<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>
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<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>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4.033&#8491;</td></tr>
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<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>
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<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>
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<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>
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</table>
</table>
== Disease ==
== Disease ==
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[[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.
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[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 ==
== Function ==
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[[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>
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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<ref>PMID:25288775</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4r3z" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Arginine--tRNA ligase]]
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[[Category: Homo sapiens]]
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[[Category: Human]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Cho, Y]]
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[[Category: Cho Y]]
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[[Category: Fu, Y]]
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[[Category: Fu Y]]
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[[Category: Kim, Y]]
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[[Category: Kim Y]]
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[[Category: Amino-acyl trna synthetase complex]]
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[[Category: Ligation amino acid to trna]]
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[[Category: Multi-synthetase complex]]
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[[Category: Protein binding-ligase complex]]
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Current revision

Crystal structure of human ArgRS-GlnRS-AIMP1 complex

PDB ID 4r3z

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