3v26
From Proteopedia
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===Crystal structure of HPF bound to the 70S ribosome. This PDB entry contains coordinates for the 30S subunit with bound HPF of the 1st ribosome in the ASU=== | ===Crystal structure of HPF bound to the 70S ribosome. This PDB entry contains coordinates for the 30S subunit with bound HPF of the 1st ribosome in the ASU=== | ||
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| + | The line below this paragraph, {{ABSTRACT_PUBMED_22605777}}, adds the Publication Abstract to the page | ||
| + | (as it appears on PubMed at http://www.pubmed.gov), where 22605777 is the PubMed ID number. | ||
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==About this Structure== | ==About this Structure== | ||
[[3v26]] is a 22 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V26 OCA]. | [[3v26]] is a 22 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V26 OCA]. | ||
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| + | ==Reference== | ||
| + | <ref group="xtra">PMID:022605777</ref><references group="xtra"/> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Thermus thermophilus]] | [[Category: Thermus thermophilus]] | ||
Revision as of 04:59, 30 May 2012
Crystal structure of HPF bound to the 70S ribosome. This PDB entry contains coordinates for the 30S subunit with bound HPF of the 1st ribosome in the ASU
Template:ABSTRACT PUBMED 22605777
About this Structure
3v26 is a 22 chain structure with sequence from Escherichia coli and Thermus thermophilus. Full crystallographic information is available from OCA.
Reference
- Polikanov YS, Blaha GM, Steitz TA. How hibernation factors RMF, HPF, and YfiA turn off protein synthesis. Science. 2012 May 18;336(6083):915-8. PMID:22605777 doi:10.1126/science.1218538
