1sb7
From Proteopedia
(New page: 200px<br /><applet load="1sb7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sb7, resolution 2.20Å" /> '''Crystal structure of...) |
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| - | [[Image:1sb7.jpg|left|200px]]<br /><applet load="1sb7" size=" | + | [[Image:1sb7.jpg|left|200px]]<br /><applet load="1sb7" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1sb7, resolution 2.20Å" /> | caption="1sb7, resolution 2.20Å" /> | ||
'''Crystal structure of the E.coli pseudouridine synthase TruD'''<br /> | '''Crystal structure of the E.coli pseudouridine synthase TruD'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The pseudouridine (Psi) synthases Pus7p and TruD define a family of | + | The pseudouridine (Psi) synthases Pus7p and TruD define a family of RNA-modifying enzymes with no sequence similarity to previously characterized Psi synthases. The 2.2 A resolution structure of Escherichia coli TruD reveals a U-shaped molecule with a catalytic domain that superimposes closely on that of other Psi synthases. A domain that appears to be unique to TruD/Pus7p family enzymes hinges over the catalytic domain, possibly serving to clasp the substrate RNAs. The active site comprises residues that are conserved in other Psi synthases, although at least one comes from a structurally distinct part of the protein. Remarkably, the connectivity of the structural elements of the TruD catalytic domain is a circular permutation of that of its paralogs. Because the sequence of the permuted segment, a beta-strand that bisects the catalytic domain, is conserved among orthologs from bacteria, archaea and eukarya, the permutation likely happened early in evolution. |
==About this Structure== | ==About this Structure== | ||
| - | 1SB7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with PO4 and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. 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:// | + | 1SB7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=PO4:'>PO4</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1SB7 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Pseudouridylate synthase]] | [[Category: Pseudouridylate synthase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Amare, A | + | [[Category: Amare, A R.Ferre-D.]] |
[[Category: Hoang, C.]] | [[Category: Hoang, C.]] | ||
[[Category: GOL]] | [[Category: GOL]] | ||
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[[Category: pseudouridine synthase]] | [[Category: pseudouridine synthase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:59:44 2008'' |
Revision as of 12:59, 21 February 2008
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Crystal structure of the E.coli pseudouridine synthase TruD
Overview
The pseudouridine (Psi) synthases Pus7p and TruD define a family of RNA-modifying enzymes with no sequence similarity to previously characterized Psi synthases. The 2.2 A resolution structure of Escherichia coli TruD reveals a U-shaped molecule with a catalytic domain that superimposes closely on that of other Psi synthases. A domain that appears to be unique to TruD/Pus7p family enzymes hinges over the catalytic domain, possibly serving to clasp the substrate RNAs. The active site comprises residues that are conserved in other Psi synthases, although at least one comes from a structurally distinct part of the protein. Remarkably, the connectivity of the structural elements of the TruD catalytic domain is a circular permutation of that of its paralogs. Because the sequence of the permuted segment, a beta-strand that bisects the catalytic domain, is conserved among orthologs from bacteria, archaea and eukarya, the permutation likely happened early in evolution.
About this Structure
1SB7 is a Single protein structure of sequence from Escherichia coli with and as ligands. Active as Pseudouridylate synthase, with EC number 4.2.1.70 Full crystallographic information is available from OCA.
Reference
Crystal structure of the highly divergent pseudouridine synthase TruD reveals a circular permutation of a conserved fold., Hoang C, Ferre-D'Amare AR, RNA. 2004 Jul;10(7):1026-33. PMID:15208439
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