1r3f

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(New page: 200px<br /><applet load="1r3f" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r3f, resolution 1.85&Aring;" /> '''Crystal Structure of...)
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'''Crystal Structure of tRNA Pseudouridine Synthase TruB and Its RNA Complex: RNA-protein Recognition Through a Combination of Rigid Docking and Induced Fit'''<br />
'''Crystal Structure of tRNA Pseudouridine Synthase TruB and Its RNA Complex: RNA-protein Recognition Through a Combination of Rigid Docking and Induced Fit'''<br />
==Overview==
==Overview==
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RNA pseudouridine synthase, TruB, catalyzes pseudouridine formation at U55, in tRNA. This posttranscriptional modification is almost universally, conserved and occurs in the T arm of most tRNAs. We determined the crystal, structure of Escherichia coli TruB apo enzyme, as well as the structure of, Thermotoga maritima TruB in complex with RNA. Comparison of the RNA-free, and -bound forms of TruB reveals that this enzyme undergoes significant, conformational changes on binding to its substrate. These conformational, changes include the ordering of the "thumb loop," which binds right into, the RNA hairpin loop, and a 10 degree hinge movement of the C-terminal, domain. Along with the result of docking experiments performed on apo, TruB, we conclude that TruB recognizes its RNA substrate through a, combination of rigid docking and induced fit, with TruB first rigidly, binding to its target and then maximizing the interaction by induced fit.
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RNA pseudouridine synthase, TruB, catalyzes pseudouridine formation at U55 in tRNA. This posttranscriptional modification is almost universally conserved and occurs in the T arm of most tRNAs. We determined the crystal structure of Escherichia coli TruB apo enzyme, as well as the structure of Thermotoga maritima TruB in complex with RNA. Comparison of the RNA-free and -bound forms of TruB reveals that this enzyme undergoes significant conformational changes on binding to its substrate. These conformational changes include the ordering of the "thumb loop," which binds right into the RNA hairpin loop, and a 10 degree hinge movement of the C-terminal domain. Along with the result of docking experiments performed on apo TruB, we conclude that TruB recognizes its RNA substrate through a combination of rigid docking and induced fit, with TruB first rigidly binding to its target and then maximizing the interaction by induced fit.
==About this Structure==
==About this Structure==
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1R3F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Pseudouridylate_synthase Pseudouridylate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.70 4.2.1.70] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1R3F OCA].
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1R3F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Pseudouridylate_synthase Pseudouridylate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.70 4.2.1.70] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R3F OCA].
==Reference==
==Reference==
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[[Category: Agarwalla, S.]]
[[Category: Agarwalla, S.]]
[[Category: Finer-Moore, J.]]
[[Category: Finer-Moore, J.]]
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[[Category: Moustakas, D.T.]]
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[[Category: Moustakas, D T.]]
[[Category: Pan, H.]]
[[Category: Pan, H.]]
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[[Category: Stroud, R.M.]]
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[[Category: Stroud, R M.]]
[[Category: pseudouridylation]]
[[Category: pseudouridylation]]
[[Category: rna modification]]
[[Category: rna modification]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:14:36 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:46:42 2008''

Revision as of 12:46, 21 February 2008


1r3f, resolution 1.85Å

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Crystal Structure of tRNA Pseudouridine Synthase TruB and Its RNA Complex: RNA-protein Recognition Through a Combination of Rigid Docking and Induced Fit

Overview

RNA pseudouridine synthase, TruB, catalyzes pseudouridine formation at U55 in tRNA. This posttranscriptional modification is almost universally conserved and occurs in the T arm of most tRNAs. We determined the crystal structure of Escherichia coli TruB apo enzyme, as well as the structure of Thermotoga maritima TruB in complex with RNA. Comparison of the RNA-free and -bound forms of TruB reveals that this enzyme undergoes significant conformational changes on binding to its substrate. These conformational changes include the ordering of the "thumb loop," which binds right into the RNA hairpin loop, and a 10 degree hinge movement of the C-terminal domain. Along with the result of docking experiments performed on apo TruB, we conclude that TruB recognizes its RNA substrate through a combination of rigid docking and induced fit, with TruB first rigidly binding to its target and then maximizing the interaction by induced fit.

About this Structure

1R3F is a Single protein structure of sequence from Escherichia coli. Active as Pseudouridylate synthase, with EC number 4.2.1.70 Full crystallographic information is available from OCA.

Reference

Structure of tRNA pseudouridine synthase TruB and its RNA complex: RNA recognition through a combination of rigid docking and induced fit., Pan H, Agarwalla S, Moustakas DT, Finer-Moore J, Stroud RM, Proc Natl Acad Sci U S A. 2003 Oct 28;100(22):12648-53. Epub 2003 Oct 17. PMID:14566049

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