1p9y
From Proteopedia
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|PDB= 1p9y |SIZE=350|CAPTION= <scene name='initialview01'>1p9y</scene>, resolution 2.15Å | |PDB= 1p9y |SIZE=350|CAPTION= <scene name='initialview01'>1p9y</scene>, resolution 2.15Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand=ACY:ACETIC ACID'>ACY</scene> | + | |LIGAND= <scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene> |
- | |ACTIVITY= [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] | + | |ACTIVITY= <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> |
|GENE= TIG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= TIG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY=[[1oms|1OMS]] | ||
+ | |RESOURCES=<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.ebi.ac.uk/pdbsum/1p9y PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1p9y RCSB]</span> | ||
}} | }} | ||
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[[Category: Gajhede, M.]] | [[Category: Gajhede, M.]] | ||
[[Category: Kristensen, O.]] | [[Category: Kristensen, O.]] | ||
- | [[Category: ACY]] | ||
[[Category: alpha-beta protein]] | [[Category: alpha-beta protein]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:56:59 2008'' |
Revision as of 19:57, 30 March 2008
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, resolution 2.15Å | |||||||
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Ligands: | |||||||
Gene: | TIG (Escherichia coli) | ||||||
Activity: | Peptidylprolyl isomerase, with EC number 5.2.1.8 | ||||||
Related: | 1OMS
| ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Ribosome binding of E. coli Trigger Factor mutant F44L.
Overview
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
1P9Y is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Chaperone binding at the ribosomal exit tunnel., Kristensen O, Gajhede M, Structure. 2003 Dec;11(12):1547-56. PMID:14656439
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