1dmg
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1dmg |SIZE=350|CAPTION= <scene name='initialview01'>1dmg</scene>, resolution 1.7Å | |PDB= 1dmg |SIZE=350|CAPTION= <scene name='initialview01'>1dmg</scene>, resolution 1.7Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CIT:CITRIC ACID'>CIT</scene> | + | |LIGAND= <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dmg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dmg OCA], [http://www.ebi.ac.uk/pdbsum/1dmg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dmg RCSB]</span> | ||
}} | }} | ||
| Line 25: | Line 28: | ||
[[Category: Wahl, M C.]] | [[Category: Wahl, M C.]] | ||
[[Category: Worbs, M.]] | [[Category: Worbs, M.]] | ||
| - | [[Category: CIT]] | ||
[[Category: alpha-beta]] | [[Category: alpha-beta]] | ||
[[Category: l4]] | [[Category: l4]] | ||
| Line 33: | Line 35: | ||
[[Category: s10 operon]] | [[Category: s10 operon]] | ||
| - | ''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 19:44:25 2008'' |
Revision as of 16:44, 30 March 2008
| |||||||
| , resolution 1.7Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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 Sun Mar 30 19:44:25 2008
Categories: Single protein | Thermotoga maritima | Huber, R. | Wahl, M C. | Worbs, M. | Alpha-beta | L4 | Ribosomal protein | Ribosome | Rna | S10 operon
