1ad2
From Proteopedia
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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 with SO4, HG and MRD as ligands. 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 Tue Nov 20 10:45:58 2007
Categories: Single protein | Thermus thermophilus | Al-Karadaghi, S. | Eliseikina, I. | Fomenkova, N. | Garber, M. | Jonsson, B.H. | Liljas, A. | Nevskaya, N. | Nikonov, S. | Ossina, N. | Unge, J. | HG | MRD | SO4 | Mutant | Protein synthesis | Ribosomal protein | Rna binding
