1ad2
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1ad2 |SIZE=350|CAPTION= <scene name='initialview01'>1ad2</scene>, resolution 1.9Å | |PDB= 1ad2 |SIZE=350|CAPTION= <scene name='initialview01'>1ad2</scene>, resolution 1.9Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ad2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ad2 OCA], [http://www.ebi.ac.uk/pdbsum/1ad2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ad2 RCSB]</span> | ||
}} | }} | ||
| Line 32: | Line 35: | ||
[[Category: Ossina, N.]] | [[Category: Ossina, N.]] | ||
[[Category: Unge, J.]] | [[Category: Unge, J.]] | ||
| - | [[Category: HG]] | ||
| - | [[Category: MRD]] | ||
| - | [[Category: SO4]] | ||
[[Category: mutant]] | [[Category: mutant]] | ||
[[Category: protein synthesis]] | [[Category: protein synthesis]] | ||
| Line 40: | Line 40: | ||
[[Category: rna binding]] | [[Category: rna binding]] | ||
| - | ''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 18:37:46 2008'' |
Revision as of 15:37, 30 March 2008
| |||||||
| , resolution 1.9Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
RIBOSOMAL PROTEIN L1 MUTANT WITH SERINE 179 REPLACED BY CYSTEINE
Overview
The crystal structure of the mutant S179C of the ribosomal protein L1 from Thermus thermophilus has been determined at 1.9 A resolution. The mutant molecule displays a small but significant opening of the cavity between the two domains. The domain movement seems to be facilitated by the flexibility of at least two conserved glycines. These glycines may be necessary for the larger conformational change needed for an induced fit mechanism upon binding RNA. The domain movement makes a disulfide bridge possible between the incorporated cysteines in two monomers of the mutant L1.
About this Structure
1AD2 is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.
Reference
A mutant form of the ribosomal protein L1 reveals conformational flexibility., Unge J, Al-Karadaghi S, Liljas A, Jonsson BH, Eliseikina I, Ossina N, Nevskaya N, Fomenkova N, Garber M, Nikonov S, FEBS Lett. 1997 Jul 7;411(1):53-9. PMID:9247141
Page seeded by OCA on Sun Mar 30 18:37:46 2008
