1p9y

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:22, 25 October 2023) (edit) (undo)
 
(6 intermediate revisions not shown.)
Line 1: Line 1:
-
{{STRUCTURE_1p9y| PDB=1p9y | SCENE= }}
 
-
===Ribosome binding of E. coli Trigger Factor mutant F44L.===
 
-
{{ABSTRACT_PUBMED_14656439}}
 
-
==Function==
+
==Ribosome binding of E. coli Trigger Factor mutant F44L.==
-
[[http://www.uniprot.org/uniprot/TIG_ECOLI TIG_ECOLI]] Involved in protein export. Acts as a chaperone by maintaining the newly synthesized secretory and non-secretory proteins in an open conformation. Binds to nascent polypeptide chains via ribosomal protein L23 (PubMed:12226666). Functions as a peptidyl-prolyl cis-trans isomerase in vitro, this activity is dispensible in vivo for chaperone activity.<ref>PMID:8633085</ref> <ref>PMID:8521806</ref> <ref>PMID:14726952</ref>
+
<StructureSection load='1p9y' size='340' side='right'caption='[[1p9y]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1p9y]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P9Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P9Y FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene></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=1p9y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p9y OCA], [https://pdbe.org/1p9y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p9y RCSB], [https://www.ebi.ac.uk/pdbsum/1p9y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p9y ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/TIG_ECOLI TIG_ECOLI] Involved in protein export. Acts as a chaperone by maintaining the newly synthesized secretory and non-secretory proteins in an open conformation. Binds to nascent polypeptide chains via ribosomal protein L23 (PubMed:12226666). Functions as a peptidyl-prolyl cis-trans isomerase in vitro, this activity is dispensible in vivo for chaperone activity.<ref>PMID:8633085</ref> <ref>PMID:8521806</ref> <ref>PMID:14726952</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/p9/1p9y_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=1p9y ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The exit tunnel region of the ribosome is well established as a focal point for interaction between the components that guide the fate of nascent polypeptides. One of these, the chaperone trigger factor (TF), associates with the 50S ribosomal subunit through its N-terminal domain. Targeting of TF to ribosomes is crucial to achieve its remarkable efficiency in protein folding. A similar tight coupling to translation is found in signal recognition particle (SRP)-dependent protein translocation. Here, we report crystal structures of the E. coli TF ribosome binding domain. TF is structurally related to the Hsp33 chaperone but has a prominent ribosome anchor located as a tip of the molecule. This tip includes the previously established unique TF signature motif. Comparison reveals that this feature is not found in SRP structures. We identify a conserved helical kink as a hallmark of the TF structure that is most likely critical to ensure ribosome association.
-
==About this Structure==
+
Chaperone binding at the ribosomal exit tunnel.,Kristensen O, Gajhede M Structure. 2003 Dec;11(12):1547-56. PMID:14656439<ref>PMID:14656439</ref>
-
[[1p9y]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P9Y OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
<ref group="xtra">PMID:014656439</ref><references group="xtra"/><references/>
+
</div>
-
[[Category: Bacillus coli migula 1895]]
+
<div class="pdbe-citations 1p9y" style="background-color:#fffaf0;"></div>
-
[[Category: Peptidylprolyl isomerase]]
+
== References ==
-
[[Category: Gajhede, M.]]
+
<references/>
-
[[Category: Kristensen, O.]]
+
__TOC__
-
[[Category: Alpha-beta protein]]
+
</StructureSection>
-
[[Category: Isomerase]]
+
[[Category: Escherichia coli]]
 +
[[Category: Large Structures]]
 +
[[Category: Gajhede M]]
 +
[[Category: Kristensen O]]

Current revision

Ribosome binding of E. coli Trigger Factor mutant F44L.

PDB ID 1p9y

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/1p9y"
Personal tools