1ze2
From Proteopedia
(New page: 200px<br /><applet load="1ze2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ze2, resolution 3.0Å" /> '''Conformational change...) |
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| - | [[Image:1ze2.gif|left|200px]]<br /><applet load="1ze2" size=" | + | [[Image:1ze2.gif|left|200px]]<br /><applet load="1ze2" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ze2, resolution 3.0Å" /> | caption="1ze2, resolution 3.0Å" /> | ||
'''Conformational change of pseudouridine 55 synthase upon its association with RNA substrate'''<br /> | '''Conformational change of pseudouridine 55 synthase upon its association with RNA substrate'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Pseudouridine 55 synthase (Psi55S) catalyzes isomerization of uridine (U) | + | Pseudouridine 55 synthase (Psi55S) catalyzes isomerization of uridine (U) to pseudouridine (Psi) at position 55 in transfer RNA. The crystal structures of Thermotoga maritima Psi55S, and its complex with RNA, have been determined at 2.9 and 3.0 A resolutions, respectively. Structural comparisons with other families of pseudouridine synthases (PsiS) indicate that Psi55S may acquire its ability to recognize a stem-loop RNA substrate by two insertions of polypeptides into the PsiS core. The structure of apo-Psi55S reveals that these two insertions interact with each other. However, association with RNA substrate induces substantial conformational change in one of the insertions, resulting in disruption of interaction between insertions and association of both insertions with the RNA substrate. Specific interactions between two insertions, as well as between the insertions and the RNA substrate, account for the molecular basis of the conformational change. |
==About this Structure== | ==About this Structure== | ||
| - | 1ZE2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. 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:// | + | 1ZE2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. 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=1ZE2 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
| - | [[Category: Huang, R | + | [[Category: Huang, R H.]] |
[[Category: Phannachet, K.]] | [[Category: Phannachet, K.]] | ||
[[Category: protein-rna complex]] | [[Category: protein-rna complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:14:37 2008'' |
Revision as of 14:14, 21 February 2008
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Conformational change of pseudouridine 55 synthase upon its association with RNA substrate
Overview
Pseudouridine 55 synthase (Psi55S) catalyzes isomerization of uridine (U) to pseudouridine (Psi) at position 55 in transfer RNA. The crystal structures of Thermotoga maritima Psi55S, and its complex with RNA, have been determined at 2.9 and 3.0 A resolutions, respectively. Structural comparisons with other families of pseudouridine synthases (PsiS) indicate that Psi55S may acquire its ability to recognize a stem-loop RNA substrate by two insertions of polypeptides into the PsiS core. The structure of apo-Psi55S reveals that these two insertions interact with each other. However, association with RNA substrate induces substantial conformational change in one of the insertions, resulting in disruption of interaction between insertions and association of both insertions with the RNA substrate. Specific interactions between two insertions, as well as between the insertions and the RNA substrate, account for the molecular basis of the conformational change.
About this Structure
1ZE2 is a Single protein structure of sequence from Thermotoga maritima. Active as Pseudouridylate synthase, with EC number 4.2.1.70 Full crystallographic information is available from OCA.
Reference
Conformational change of pseudouridine 55 synthase upon its association with RNA substrate., Phannachet K, Huang RH, Nucleic Acids Res. 2004 Feb 27;32(4):1422-9. Print 2004. PMID:14990747
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