1ad2

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(New page: 200px<br /><applet load="1ad2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ad2, resolution 1.9&Aring;" /> '''RIBOSOMAL PROTEIN L1 ...)
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[[Image:1ad2.gif|left|200px]]<br /><applet load="1ad2" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ad2.gif|left|200px]]<br /><applet load="1ad2" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ad2, resolution 1.9&Aring;" />
caption="1ad2, resolution 1.9&Aring;" />
'''RIBOSOMAL PROTEIN L1 MUTANT WITH SERINE 179 REPLACED BY CYSTEINE'''<br />
'''RIBOSOMAL PROTEIN L1 MUTANT WITH SERINE 179 REPLACED BY CYSTEINE'''<br />
==Overview==
==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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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==
==About this Structure==
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1AD2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with SO4, HG and MRD as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AD2 OCA].
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1AD2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=HG:'>HG</scene> and <scene name='pdbligand=MRD:'>MRD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AD2 OCA].
==Reference==
==Reference==
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[[Category: Fomenkova, N.]]
[[Category: Fomenkova, N.]]
[[Category: Garber, M.]]
[[Category: Garber, M.]]
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[[Category: Jonsson, B.H.]]
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[[Category: Jonsson, B H.]]
[[Category: Liljas, A.]]
[[Category: Liljas, A.]]
[[Category: Nevskaya, N.]]
[[Category: Nevskaya, N.]]
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[[Category: rna binding]]
[[Category: rna binding]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:45:58 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:43:15 2008''

Revision as of 09:43, 21 February 2008

Image:1ad2.gif

1ad2, resolution 1.9Å

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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 , and 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

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