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1hk9
From Proteopedia
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| - | [[Image:1hk9.jpg|left|200px]] | + | [[Image:1hk9.jpg|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF THE HFQ PROTEIN FROM ESCHERICHIA COLI''' | + | {{Structure |
| + | |PDB= 1hk9 |SIZE=350|CAPTION= <scene name='initialview01'>1hk9</scene>, resolution 2.15Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''CRYSTAL STRUCTURE OF THE HFQ PROTEIN FROM ESCHERICHIA COLI''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1HK9 is a [ | + | 1HK9 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=1HK9 OCA]. |
==Reference== | ==Reference== | ||
| - | Sm-like proteins in Eubacteria: the crystal structure of the Hfq protein from Escherichia coli., Sauter C, Basquin J, Suck D, Nucleic Acids Res. 2003 Jul 15;31(14):4091-8. PMID:[http:// | + | Sm-like proteins in Eubacteria: the crystal structure of the Hfq protein from Escherichia coli., Sauter C, Basquin J, Suck D, Nucleic Acids Res. 2003 Jul 15;31(14):4091-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12853626 12853626] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: sm-like]] | [[Category: sm-like]] | ||
| - | ''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 11:38:10 2008'' |
Revision as of 09:38, 20 March 2008
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| , resolution 2.15Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE HFQ PROTEIN FROM ESCHERICHIA COLI
Overview
The Hfq protein was discovered in Escherichia coli in the early seventies as a host factor for the Qbeta phage RNA replication. During the last decade, it was shown to be involved in many RNA processing events and remote sequence homology indicated a link to spliceosomal Sm proteins. We report the crystal structure of the E.coli Hfq protein showing that its monomer displays a characteristic Sm-fold and forms a homo-hexamer, in agreement with former biochemical data. Overall, the structure of the E.coli Hfq ring is similar to the one recently described for Staphylococcus aureus. This confirms that bacteria contain a hexameric Sm-like protein which is likely to be an ancient and less specialized form characterized by a relaxed RNA binding specificity. In addition, we identified an Hfq ortholog in the archaeon Methanococcus jannaschii which lacks a classical Sm/Lsm gene. Finally, a detailed structural comparison shows that the Sm-fold is remarkably well conserved in bacteria, Archaea and Eukarya, and represents a universal and modular building unit for oligomeric RNA binding proteins.
About this Structure
1HK9 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Sm-like proteins in Eubacteria: the crystal structure of the Hfq protein from Escherichia coli., Sauter C, Basquin J, Suck D, Nucleic Acids Res. 2003 Jul 15;31(14):4091-8. PMID:12853626
Page seeded by OCA on Thu Mar 20 11:38:10 2008
