1ze2

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[[Image:1ze2.gif|left|200px]]<br /><applet load="1ze2" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ze2.gif|left|200px]]
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caption="1ze2, resolution 3.0&Aring;" />
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'''Conformational change of pseudouridine 55 synthase upon its association with RNA substrate'''<br />
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{{Structure
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|PDB= 1ze2 |SIZE=350|CAPTION= <scene name='initialview01'>1ze2</scene>, resolution 3.0&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY= [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]
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|GENE= truB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 Thermotoga maritima])
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}}
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'''Conformational change of pseudouridine 55 synthase upon its association with RNA substrate'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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1ZE2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZE2 OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14990747 14990747]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/14990747 14990747]
[[Category: Pseudouridylate synthase]]
[[Category: Pseudouridylate synthase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: protein-rna complex]]
[[Category: protein-rna complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:14:37 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:34:21 2008''

Revision as of 13:34, 20 March 2008


PDB ID 1ze2

Drag the structure with the mouse to rotate
, resolution 3.0Å
Gene: truB (Thermotoga maritima)
Activity: Pseudouridylate synthase, with EC number 4.2.1.70
Coordinates: save as pdb, mmCIF, xml



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. 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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