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4ojm

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Revision as of 11:40, 4 August 2016

Crystal structure of a C-terminally truncated CYT-18 protein including N-terminal residues

Structural highlights

4ojm is a 1 chain structure with sequence from Neucr. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1y42
Gene:	cyt-18, B18P24.070, NCU03030 (NEUCR)
Activity:	Tyrosine--tRNA ligase, with EC number 6.1.1.1
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[SYYM_NEUCR] Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr). Has both an aminoacyl-tRNA synthetase activity and is involved in the splicing of group I introns. It acts in intron splicing by stabilizing the catalytically active structure of the intron.

Publication Abstract from PubMed

The mitochondrial tyrosyl tRNA synthetase from Neurospora crassa (CYT-18 protein) is a bifunctional group I intron splicing cofactor. CYT-18 is capable of splicing multiple group I introns from a wide variety of sources by stabilizing the catalytically active intron structures. CYT-18 and mt TyrRSs from related fungal species have evolved to assist in group I intron splicing in part by the accumulation of three N-terminal domain insertions. Biochemical and structural analysis indicate that the N-terminal insertions serve primarily to create a structure-stabilizing scaffold for critical tertiary interactions between the two major RNA domains of group I introns. Previous studies concluded that the primarily alpha-helical N-terminal insertion, H0, contributes to protein stability and is necessary for splicing the N. crassa ND1 intron but is dispensable for splicing the N. crassa mitochondrial LSU intron. Here, we show that CYT-18 with a complete H0 deletion retains residual ND1 intron splicing activity and that addition of the missing N-terminus in trans is capable of restoring a significant portion of its splicing activity. The development of this peptide complementation assay has allowed us to explore important characteristics of the CYT-18/group I intron interaction including the stoichiometry of H0 in intron splicing and the importance of specific H0 residues. Evaluation of truncated H0 peptides in this assay and a re-examination of the CYT-18 crystal structure suggest a previously unknown structural role of the first five N-terminal residues of CYT-18. These residues interact directly with another splicing insertion, making H0 a central structural element responsible for connecting all three N-terminal splicing insertions.

An in vitro peptide complementation assay for CYT-18-dependent group I intron splicing reveals a new role for the N-terminus.,Geng C, Paukstelis PJ Biochemistry. 2014 Mar 4;53(8):1311-9. doi: 10.1021/bi401614h. Epub 2014 Feb 24. PMID:24520960^[1]

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

References

↑ Geng C, Paukstelis PJ. An in vitro peptide complementation assay for CYT-18-dependent group I intron splicing reveals a new role for the N-terminus. Biochemistry. 2014 Mar 4;53(8):1311-9. doi: 10.1021/bi401614h. Epub 2014 Feb 24. PMID:24520960 doi:http://dx.doi.org/10.1021/bi401614h

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/4ojm"

@@ Line 1: / Line 1: @@
 ==Crystal structure of a C-terminally truncated CYT-18 protein including N-terminal residues==
 <StructureSection load='4ojm' size='340' side='right' caption='[[4ojm]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
@@ Line 7: / Line 8: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cyt-18, B18P24.070, NCU03030 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=367110 NEUCR])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tyrosine--tRNA_ligase Tyrosine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.1 6.1.1.1] </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=4ojm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ojm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ojm RCSB], [http://www.ebi.ac.uk/pdbsum/4ojm PDBsum]</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=4ojm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ojm OCA], [http://pdbe.org/4ojm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ojm RCSB], [http://www.ebi.ac.uk/pdbsum/4ojm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ojm ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 19: / Line 20: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4ojm" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4ojm

From Proteopedia

Revision as of 11:40, 4 August 2016

Crystal structure of a C-terminally truncated CYT-18 protein including N-terminal residues

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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