1ad2

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{{STRUCTURE_1ad2| PDB=1ad2 | SCENE= }}
{{STRUCTURE_1ad2| PDB=1ad2 | SCENE= }}
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'''RIBOSOMAL PROTEIN L1 MUTANT WITH SERINE 179 REPLACED BY CYSTEINE'''
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===RIBOSOMAL PROTEIN L1 MUTANT WITH SERINE 179 REPLACED BY CYSTEINE===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 9247141 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9247141}}
==About this Structure==
==About this Structure==
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[[Category: Ribosomal protein]]
[[Category: Ribosomal protein]]
[[Category: Rna binding]]
[[Category: Rna binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 16:36:05 2008''

Revision as of 13:36, 30 June 2008

Image:1ad2.png

Template:STRUCTURE 1ad2

RIBOSOMAL PROTEIN L1 MUTANT WITH SERINE 179 REPLACED BY CYSTEINE

Template:ABSTRACT PUBMED 9247141

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

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