1y42

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of a C-terminally truncated CYT-18 protein

Structural highlights

1y42 is a 1 chain structure with sequence from Neurospora crassa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.95Å
Ligands:
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.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

We determined a 1.95 A X-ray crystal structure of a C-terminally truncated Neurospora crassa mitochondrial tyrosyl-tRNA synthetase (CYT-18 protein) that functions in splicing group I introns. CYT-18's nucleotide binding fold and intermediate alpha-helical domains superimpose on those of bacterial TyrRSs, except for an N-terminal extension and two small insertions not found in nonsplicing bacterial enzymes. These additions surround the cyt-18-1 mutation site and are sites of suppressor mutations that restore splicing, but not synthetase activity. Highly constrained models based on directed hydroxyl radical cleavage assays show that the group I intron binds at a site formed in part by the three additions on the nucleotide binding fold surface opposite that which binds tRNATyr. Our results show how essential proteins can progressively evolve new functions.

A tyrosyl-tRNA synthetase adapted to function in group I intron splicing by acquiring a new RNA binding surface.,Paukstelis PJ, Coon R, Madabusi L, Nowakowski J, Monzingo A, Robertus J, Lambowitz AM Mol Cell. 2005 Feb 4;17(3):417-28. PMID:15694342^[1]

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

References

↑ Paukstelis PJ, Coon R, Madabusi L, Nowakowski J, Monzingo A, Robertus J, Lambowitz AM. A tyrosyl-tRNA synthetase adapted to function in group I intron splicing by acquiring a new RNA binding surface. Mol Cell. 2005 Feb 4;17(3):417-28. PMID:15694342 doi:10.1016/j.molcel.2004.12.026

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1y42"

@@ Line 3: / Line 3: @@
 <StructureSection load='1y42' size='340' side='right'caption='[[1y42]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1y42]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chrysonilia_crassa Chrysonilia crassa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y42 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1Y42 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1y42]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Neurospora_crassa Neurospora crassa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y42 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y42 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TYR:TYROSINE'>TYR</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cyt-18 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5141 Chrysonilia crassa])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TYR:TYROSINE'>TYR</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=1y42 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y42 OCA], [https://pdbe.org/1y42 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y42 RCSB], [https://www.ebi.ac.uk/pdbsum/1y42 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y42 ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1y42 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y42 OCA], [http://pdbe.org/1y42 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1y42 RCSB], [http://www.ebi.ac.uk/pdbsum/1y42 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1y42 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/SYYM_NEUCR 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.
+[https://www.uniprot.org/uniprot/SYYM_NEUCR 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.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 37: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Chrysonilia crassa]]
 [[Category: Large Structures]]
-[[Category: Tyrosine--tRNA ligase]]
+[[Category: Neurospora crassa]]
-[[Category: Coon, R]]
+[[Category: Coon R]]
-[[Category: Lambowitz, A M]]
+[[Category: Lambowitz AM]]
-[[Category: Madabusi, L]]
+[[Category: Madabusi L]]
-[[Category: Monzingo, A]]
+[[Category: Monzingo A]]
-[[Category: Nowakowski, J]]
+[[Category: Nowakowski J]]
-[[Category: Paukstelis, P J]]
+[[Category: Paukstelis PJ]]
-[[Category: Robertus, J]]
+[[Category: Robertus J]]
-[[Category: Cyt-18]]
-[[Category: Group i intron]]
-[[Category: Ligase]]
-[[Category: Trna ligase]]
-[[Category: Tyrosyl trna synthetase]]

1y42

From Proteopedia

Current revision

Crystal structure of a C-terminally truncated CYT-18 protein

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox