This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


3hfv

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:21, 6 September 2023) (edit) (undo)
 
(8 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:3hfv.jpg|left|200px]]
 
-
<!--
+
==Crystal structure of human mitochondrial phenylalanyl-tRNA synthetase complexed with m-tyrosine==
-
The line below this paragraph, containing "STRUCTURE_3hfv", creates the "Structure Box" on the page.
+
<StructureSection load='3hfv' size='340' side='right'caption='[[3hfv]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[3hfv]] is a 1 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=3HFV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HFV FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
-
-->
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MTY:META-TYROSINE'>MTY</scene></td></tr>
-
{{STRUCTURE_3hfv| PDB=3hfv | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3hfv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hfv OCA], [https://pdbe.org/3hfv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hfv RCSB], [https://www.ebi.ac.uk/pdbsum/3hfv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hfv ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/SYFM_HUMAN SYFM_HUMAN] Catalyzes direct attachment of p-Tyr (Tyr) to tRNAPhe. Permits also, with a lower efficiency, the attachment of m-Tyr to tRNAPhe, thereby opening the way for delivery of the misacylated tRNA to the ribosome and incorporation of ROS-damaged amino acid into proteins.<ref>PMID:19549855</ref>
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hf/3hfv_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3hfv ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The accumulation of proteins damaged by reactive oxygen species (ROS), conventionally regarded as having pathological potentials, is associated with age-related diseases such as Alzheimer's, atherosclerosis, and cataractogenesis. Exposure of the aromatic amino acid phenylalanine to ROS-generating systems produces multiple isomers of tyrosine: m-tyrosine (m-Tyr), o-tyrosine (o-Tyr), and the standard p-tyrosine (Tyr). Previously it was demonstrated that exogenously supplied, oxidized amino acids could be incorporated into bacterial and eukaryotic proteins. It is, therefore, likely that in many cases, in vivo-damaged amino acids are available for de novo synthesis of proteins. Although the involvement of aminoacyl-tRNA synthetases in this process has been hypothesized, the specific pathway by which ROS-damaged amino acids are incorporated into proteins remains unclear. We provide herein evidence that mitochondrial and cytoplasmic phenylalanyl-tRNA synthetases (HsmtPheRS and HsctPheRS, respectively) catalyze direct attachment of m-Tyr to tRNA(Phe), thereby opening the way for delivery of the misacylated tRNA to the ribosome and incorporation of ROS-damaged amino acid into eukaryotic proteins. Crystal complexes of mitochondrial and bacterial PheRSs with m-Tyr reveal the net of highly specific interactions within the synthetic and editing sites.
-
===Crystal structure of human mitochondrial phenylalanyl-tRNA synthetase complexed with m-tyrosine===
+
Eukaryotic cytosolic and mitochondrial phenylalanyl-tRNA synthetases catalyze the charging of tRNA with the meta-tyrosine.,Klipcan L, Moor N, Kessler N, Safro MG Proc Natl Acad Sci U S A. 2009 Jul 7;106(27):11045-8. Epub 2009 Jun 22. PMID:19549855<ref>PMID:19549855</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 3hfv" style="background-color:#fffaf0;"></div>
-
<!--
+
==See Also==
-
The line below this paragraph, {{ABSTRACT_PUBMED_19549855}}, adds the Publication Abstract to the page
+
*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
-
(as it appears on PubMed at http://www.pubmed.gov), where 19549855 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_19549855}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
-
3HFV is a 1 chain structure of 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=3HFV OCA].
+
-
 
+
-
==Reference==
+
-
<ref group="xtra">PMID:19549855</ref><references group="xtra"/>
+
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Phenylalanine--tRNA ligase]]
+
[[Category: Large Structures]]
-
[[Category: Kessler, N.]]
+
[[Category: Kessler N]]
-
[[Category: Klipcan, L.]]
+
[[Category: Klipcan L]]
-
[[Category: Moor, N.]]
+
[[Category: Moor N]]
-
[[Category: Safro, M G.]]
+
[[Category: Safro MG]]
-
[[Category: Aminoacyl-trna synthetase]]
+
-
[[Category: Atp-binding]]
+
-
[[Category: Classii aarss fold]]
+
-
[[Category: Ligase]]
+
-
[[Category: M-tyrosine]]
+
-
[[Category: Mitochondrion]]
+
-
[[Category: Nucleotide-binding]]
+
-
[[Category: Polymorphism]]
+
-
[[Category: Protein biosynthesis]]
+
-
[[Category: Rna recogntion]]
+
-
[[Category: Rrm domain]]
+
-
[[Category: Transit peptide]]
+
-
[[Category: Trna]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 22 20:43:27 2009''
+

Current revision

Crystal structure of human mitochondrial phenylalanyl-tRNA synthetase complexed with m-tyrosine

PDB ID 3hfv

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3hfv"
Personal tools