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5bmu

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Revision as of 08:50, 11 March 2020

The crystal structure of the GST-like domains complex of AIMP3-EPRS mutant C92SC105SC123S

Structural highlights

5bmu is a 8 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	EEF1E1, AIMP3, P18 (HUMAN), EPRS (HUMAN)
Activity:	Glutamate--tRNA ligase, with EC number 6.1.1.17
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[MCA3_HUMAN] Positive modulator of ATM response to DNA damage. [SYEP_HUMAN] Catalyzes the attachment of the cognate amino acid to the corresponding tRNA in a two-step reaction: the amino acid is first activated by ATP to form a covalent intermediate with AMP and is then transferred to the acceptor end of the cognate tRNA. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma activation and subsequent phosphorylation dissociates from the multisynthetase complex and assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation.^[1] ^[2] ^[3]

Publication Abstract from PubMed

Many multi-component protein complexes mediating diverse cellular processes are assembled through scaffolds with specialized protein interaction modules. The multi-tRNA synthetase complex (MSC), consisting of nine different aminoacyl-tRNA synthetases and three non-enzymatic factors (AIMP1-3), serves as a hub for many signaling pathways in addition to its role in protein synthesis. However, the assembly process and structural arrangement of the MSC components are not well understood. Here we show the heterotetrameric complex structure of the glutathione transferase (GST) domains shared among the four MSC components, methionyl-tRNA synthetase (MRS), glutaminyl-prolyl-tRNA synthetase (EPRS), AIMP2 and AIMP3. The MRS-AIMP3 and EPRS-AIMP2 using interface 1 are bridged via interface 2 of AIMP3 and EPRS to generate a unique linear complex of MRS-AIMP3:EPRS-AIMP2 at the molar ratio of (1:1):(1:1). Interestingly, the affinity at interface 2 of AIMP3:EPRS can be varied depending on the occupancy of interface 1, suggesting dynamic nature of the linear GST tetramer. The four components are optimally arranged for maximal accommodation of additional domains and proteins. These characteristics suggest the GST tetramer as a unique and dynamic structural platform from which the MSC components are assembled. Considering prevalence of the GST-like domains, this tetramer can also provide a tool for the communication of the MSC with other GST-containing cellular factors.

Assembly of Multi-tRNA Synthetase Complex via Heterotetrameric Glutathione Transferase-Homology Domains.,Cho HY, Maeng SJ, Cho HJ, Choi YS, Chung JM, Lee S, Kim HK, Kim JH, Eom CY, Kim YG, Guo M, Jung HS, Kang BS, Kim S J Biol Chem. 2015 Oct 15. pii: jbc.M115.690867. PMID:26472928^[4]

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

References

↑ Cerini C, Kerjan P, Astier M, Gratecos D, Mirande M, Semeriva M. A component of the multisynthetase complex is a multifunctional aminoacyl-tRNA synthetase. EMBO J. 1991 Dec;10(13):4267-77. PMID:1756734
↑ Sampath P, Mazumder B, Seshadri V, Gerber CA, Chavatte L, Kinter M, Ting SM, Dignam JD, Kim S, Driscoll DM, Fox PL. Noncanonical function of glutamyl-prolyl-tRNA synthetase: gene-specific silencing of translation. Cell. 2004 Oct 15;119(2):195-208. PMID:15479637 doi:http://dx.doi.org/10.1016/j.cell.2004.09.030
↑ Arif A, Chatterjee P, Moodt RA, Fox PL. Heterotrimeric GAIT complex drives transcript-selective translation inhibition in murine macrophages. Mol Cell Biol. 2012 Dec;32(24):5046-55. doi: 10.1128/MCB.01168-12. Epub 2012 Oct , 15. PMID:23071094 doi:10.1128/MCB.01168-12
↑ Cho HY, Maeng SJ, Cho HJ, Choi YS, Chung JM, Lee S, Kim HK, Kim JH, Eom CY, Kim YG, Guo M, Jung HS, Kang BS, Kim S. Assembly of Multi-tRNA Synthetase Complex via Heterotetrameric Glutathione Transferase-Homology Domains. J Biol Chem. 2015 Oct 15. pii: jbc.M115.690867. PMID:26472928 doi:http://dx.doi.org/10.1074/jbc.M115.690867

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/5bmu"

@@ Line 1: / Line 1: @@
 ==The crystal structure of the GST-like domains complex of AIMP3-EPRS mutant C92SC105SC123S==
-<StructureSection load='5bmu' size='340' side='right' caption='[[5bmu]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
+<StructureSection load='5bmu' size='340' side='right'caption='[[5bmu]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5bmu]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BMU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5BMU FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5bmu]] is a 8 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=5BMU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5BMU FirstGlance]. <br>
-</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate--tRNA_ligase Glutamate--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.17 6.1.1.17] </span></td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EEF1E1, AIMP3, P18 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), EPRS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5bmu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bmu OCA], [http://pdbe.org/5bmu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5bmu RCSB], [http://www.ebi.ac.uk/pdbsum/5bmu PDBsum]</span></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate--tRNA_ligase Glutamate--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.17 6.1.1.17] </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=5bmu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bmu OCA], [http://pdbe.org/5bmu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5bmu RCSB], [http://www.ebi.ac.uk/pdbsum/5bmu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5bmu ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 19: @@
 </div>
 <div class="pdbe-citations 5bmu" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
+*[[Elongation factor 3D structures|Elongation factor 3D structures]]
 == References ==
 <references/>
@@ Line 22: / Line 28: @@
 </StructureSection>
 [[Category: Glutamate--tRNA ligase]]
+[[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Cho, H J]]
 [[Category: Kang, B S]]

5bmu

From Proteopedia

Revision as of 08:50, 11 March 2020

The crystal structure of the GST-like domains complex of AIMP3-EPRS mutant C92SC105SC123S

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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