1oms
From Proteopedia
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| - | [[Image:1oms.gif|left|200px]] | + | [[Image:1oms.gif|left|200px]] |
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| - | '''Structure determination by MAD: E.coli Trigger Factor binding at the ribosomal exit tunnel.''' | + | {{Structure |
| + | |PDB= 1oms |SIZE=350|CAPTION= <scene name='initialview01'>1oms</scene>, resolution 2.30Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=SO2:SULFUR+DIOXIDE'>SO2</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</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] | ||
| + | |GENE= tig ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''Structure determination by MAD: E.coli Trigger Factor binding at the ribosomal exit tunnel.''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1OMS is a [ | + | 1OMS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OMS OCA]. |
==Reference== | ==Reference== | ||
| - | Chaperone binding at the ribosomal exit tunnel., Kristensen O, Gajhede M, Structure. 2003 Dec;11(12):1547-56. PMID:[http:// | + | Chaperone binding at the ribosomal exit tunnel., Kristensen O, Gajhede M, Structure. 2003 Dec;11(12):1547-56. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14656439 14656439] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Peptidylprolyl isomerase]] | [[Category: Peptidylprolyl isomerase]] | ||
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[[Category: alpha-beta structure]] | [[Category: alpha-beta structure]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:12:52 2008'' |
Revision as of 11:12, 20 March 2008
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| , resolution 2.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , and | ||||||
| Gene: | tig (Escherichia coli) | ||||||
| Activity: | Peptidylprolyl isomerase, with EC number 5.2.1.8 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure determination by MAD: E.coli Trigger Factor binding at the ribosomal exit tunnel.
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
1OMS 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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