4j15: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Crystal structure of human cytosolic aspartyl-tRNA synthetase, a component of multi-tRNA synthetase complex== | |||
<StructureSection load='4j15' size='340' side='right' caption='[[4j15]], [[Resolution|resolution]] 2.24Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4j15]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J15 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4J15 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DARS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartate--tRNA_ligase Aspartate--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.12 6.1.1.12] </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=4j15 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j15 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4j15 RCSB], [http://www.ebi.ac.uk/pdbsum/4j15 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Human cytosolic aspartyl-tRNA synthetase (DRS) catalyzes the attachment of the amino acid aspartic acid to its cognate tRNA and it is a component of the multi-tRNA synthetase complex (MSC) which has been known to be involved in unexpected signaling pathways. Here, we report the crystal structure of DRS at 2.25 A resolution. DRS is a homodimer with a dimer interface 3,750.5 A2 which comprises of 16.6% of the monomeric surface area. Our structure reveals the C-terminal end of the N-helix which is considered as a unique addition in DRS, and its conformation further supports the switching model of the N-helix for the transfer of tRNAAsp to elongation factor 1alpha. From our analyses of the crystal structure and post-translational modification of DRS, we suggest that the phosphorylation of Ser146 provokes the separation of DRS from the MSC and provides the binding site for an interaction partner with unforeseen functions. (c) Proteins 2013;. (c) 2013 Wiley Periodicals, Inc. | |||
Crystal structure of human cytosolic aspartyl-tRNA synthetase, a component of multi-tRNA synthetase complex.,Kim KR, Park SH, Kim HS, Rhee KH, Kim BG, Kim DG, Park MS, Kim HJ, Kim S, Han BW Proteins. 2013 Apr 23. doi: 10.1002/prot.24306. PMID:23609930<ref>PMID:23609930</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Aspartate--tRNA ligase]] | [[Category: Aspartate--tRNA ligase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Han, B W | [[Category: Han, B W]] | ||
[[Category: Kim, B G | [[Category: Kim, B G]] | ||
[[Category: Kim, D G | [[Category: Kim, D G]] | ||
[[Category: Kim, H J | [[Category: Kim, H J]] | ||
[[Category: Kim, H S | [[Category: Kim, H S]] | ||
[[Category: Kim, K R | [[Category: Kim, K R]] | ||
[[Category: Kim, S | [[Category: Kim, S]] | ||
[[Category: Park, M S | [[Category: Park, M S]] | ||
[[Category: Park, S H | [[Category: Park, S H]] | ||
[[Category: Rhee, K H | [[Category: Rhee, K H]] | ||
[[Category: Aspartyl-trna synthetase]] | [[Category: Aspartyl-trna synthetase]] | ||
[[Category: Ligase]] | [[Category: Ligase]] | ||
[[Category: Trna]] | [[Category: Trna]] | ||
Revision as of 16:07, 21 December 2014
Crystal structure of human cytosolic aspartyl-tRNA synthetase, a component of multi-tRNA synthetase complexCrystal structure of human cytosolic aspartyl-tRNA synthetase, a component of multi-tRNA synthetase complex
Structural highlights
Publication Abstract from PubMedHuman cytosolic aspartyl-tRNA synthetase (DRS) catalyzes the attachment of the amino acid aspartic acid to its cognate tRNA and it is a component of the multi-tRNA synthetase complex (MSC) which has been known to be involved in unexpected signaling pathways. Here, we report the crystal structure of DRS at 2.25 A resolution. DRS is a homodimer with a dimer interface 3,750.5 A2 which comprises of 16.6% of the monomeric surface area. Our structure reveals the C-terminal end of the N-helix which is considered as a unique addition in DRS, and its conformation further supports the switching model of the N-helix for the transfer of tRNAAsp to elongation factor 1alpha. From our analyses of the crystal structure and post-translational modification of DRS, we suggest that the phosphorylation of Ser146 provokes the separation of DRS from the MSC and provides the binding site for an interaction partner with unforeseen functions. (c) Proteins 2013;. (c) 2013 Wiley Periodicals, Inc. Crystal structure of human cytosolic aspartyl-tRNA synthetase, a component of multi-tRNA synthetase complex.,Kim KR, Park SH, Kim HS, Rhee KH, Kim BG, Kim DG, Park MS, Kim HJ, Kim S, Han BW Proteins. 2013 Apr 23. doi: 10.1002/prot.24306. PMID:23609930[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||||