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1p9y

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Revision as of 14:56, 25 December 2014

Ribosome binding of E. coli Trigger Factor mutant F44L.

Structural highlights

1p9y is a 2 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1oms
Gene:	TIG ("Bacillus coli" Migula 1895)
Activity:	Peptidylprolyl isomerase, with EC number 5.2.1.8
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[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.^[1] ^[2] ^[3]

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

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.

Chaperone binding at the ribosomal exit tunnel.,Kristensen O, Gajhede M Structure. 2003 Dec;11(12):1547-56. PMID:14656439^[4]

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

References

↑ Hesterkamp T, Hauser S, Lutcke H, Bukau B. Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains. Proc Natl Acad Sci U S A. 1996 Apr 30;93(9):4437-41. PMID:8633085
↑ Valent QA, Kendall DA, High S, Kusters R, Oudega B, Luirink J. Early events in preprotein recognition in E. coli: interaction of SRP and trigger factor with nascent polypeptides. EMBO J. 1995 Nov 15;14(22):5494-505. PMID:8521806
↑ Genevaux P, Keppel F, Schwager F, Langendijk-Genevaux PS, Hartl FU, Georgopoulos C. In vivo analysis of the overlapping functions of DnaK and trigger factor. EMBO Rep. 2004 Feb;5(2):195-200. Epub 2004 Jan 9. PMID:14726952 doi:10.1038/sj.embor.7400067
↑ Kristensen O, Gajhede M. Chaperone binding at the ribosomal exit tunnel. Structure. 2003 Dec;11(12):1547-56. PMID:14656439

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1p9y"

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1P9Y FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene><br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene></td></tr>
-<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1oms|1oms]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1oms|1oms]]</td></tr>
-<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TIG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TIG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
-<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span></td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1p9y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p9y OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1p9y RCSB], [http://www.ebi.ac.uk/pdbsum/1p9y 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=1p9y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p9y OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1p9y RCSB], [http://www.ebi.ac.uk/pdbsum/1p9y PDBsum]</span></td></tr>
-<table>
+</table>
+== Function ==
+[[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>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 33: / Line 35: @@
 [[Category: Bacillus coli migula 1895]]
 [[Category: Peptidylprolyl isomerase]]
-[[Category: Gajhede, M.]]
+[[Category: Gajhede, M]]
-[[Category: Kristensen, O.]]
+[[Category: Kristensen, O]]
 [[Category: Alpha-beta protein]]
 [[Category: Isomerase]]

1p9y

From Proteopedia

Revision as of 14:56, 25 December 2014

Ribosome binding of E. coli Trigger Factor mutant F44L.

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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