1dmg
From Proteopedia
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| - | [[Image:1dmg.gif|left|200px]] | + | [[Image:1dmg.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF RIBOSOMAL PROTEIN L4''' | + | {{Structure |
| + | |PDB= 1dmg |SIZE=350|CAPTION= <scene name='initialview01'>1dmg</scene>, resolution 1.7Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CIT:CITRIC ACID'>CIT</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF RIBOSOMAL PROTEIN L4''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1DMG is a [ | + | 1DMG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DMG OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of ribosomal protein L4 shows RNA-binding sites for ribosome incorporation and feedback control of the S10 operon., Worbs M, Huber R, Wahl MC, EMBO J. 2000 Mar 1;19(5):807-18. PMID:[http:// | + | Crystal structure of ribosomal protein L4 shows RNA-binding sites for ribosome incorporation and feedback control of the S10 operon., Worbs M, Huber R, Wahl MC, EMBO J. 2000 Mar 1;19(5):807-18. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10698923 10698923] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
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[[Category: s10 operon]] | [[Category: s10 operon]] | ||
| - | ''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 10:40:53 2008'' |
Revision as of 08:40, 20 March 2008
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| , resolution 1.7Å | |||||||
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| Ligands: | |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF RIBOSOMAL PROTEIN L4
Overview
Ribosomal protein L4 resides near the peptidyl transferase center of the bacterial ribosome and may, together with rRNA and proteins L2 and L3, actively participate in the catalysis of peptide bond formation. Escherichia coli L4 is also an autogenous feedback regulator of transcription and translation of the 11 gene S10 operon. The crystal structure of L4 from Thermotoga maritima at 1.7 A resolution shows the protein with an alternating alpha/beta fold and a large disordered loop region. Two separate binding sites for RNA are discernible. The N-terminal site, responsible for binding to rRNA, consists of the disordered loop with flanking alpha-helices. The C-terminal site, a prime candidate for the interaction with the leader sequence of the S10 mRNA, involves two non-consecutive alpha-helices. The structure also suggests a C-terminal protein-binding interface, through which L4 could be interacting with protein components of the transcriptional and/or translational machineries.
About this Structure
1DMG is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.
Reference
Crystal structure of ribosomal protein L4 shows RNA-binding sites for ribosome incorporation and feedback control of the S10 operon., Worbs M, Huber R, Wahl MC, EMBO J. 2000 Mar 1;19(5):807-18. PMID:10698923
Page seeded by OCA on Thu Mar 20 10:40:53 2008
Categories: Single protein | Thermotoga maritima | Huber, R. | Wahl, M C. | Worbs, M. | CIT | Alpha-beta | L4 | Ribosomal protein | Ribosome | Rna | S10 operon

