1qyu

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caption="1qyu, resolution 2.00&Aring;" />
'''Structure of the catalytic domain of 23S rRNA pseudouridine synthase RluD'''<br />
'''Structure of the catalytic domain of 23S rRNA pseudouridine synthase RluD'''<br />
==Overview==
==Overview==
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Escherichia coli pseudouridine synthase RluD makes pseudouridines 1911, 1915, and 1917 in the loop of helix 69 in 23S RNA. These are the most, highly conserved ribosomal pseudouridines known. Of 11 pseudouridine, synthases in E. coli, only cells lacking RluD have severe growth defects, and abnormal ribosomes. We have determined the 2.0 A structure of the, catalytic domain of RluD (residues 77-326), the first structure of an RluA, family member. The catalytic domain folds into a mainly antiparallel, beta-sheet flanked by several loops and helices. A positively charged, cleft that presumably binds RNA leads to the conserved Asp 139. The RluD, N-terminal S4 domain, connected by a flexible linker, is disordered in our, structure. RluD is very similar in both catalytic domain structure and, active site arrangement to the pseudouridine synthases RsuA, TruB, and, TruA. We identify five sequence motifs, two of which are novel, in the, RluA, RsuA, TruB, and TruA families, uniting them as one superfamily., These results strongly suggest that four of the five families of, pseudouridine synthases arose by divergent evolution. The RluD structure, also provides insight into its multisite specificity.
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Escherichia coli pseudouridine synthase RluD makes pseudouridines 1911, 1915, and 1917 in the loop of helix 69 in 23S RNA. These are the most highly conserved ribosomal pseudouridines known. Of 11 pseudouridine synthases in E. coli, only cells lacking RluD have severe growth defects and abnormal ribosomes. We have determined the 2.0 A structure of the catalytic domain of RluD (residues 77-326), the first structure of an RluA family member. The catalytic domain folds into a mainly antiparallel beta-sheet flanked by several loops and helices. A positively charged cleft that presumably binds RNA leads to the conserved Asp 139. The RluD N-terminal S4 domain, connected by a flexible linker, is disordered in our structure. RluD is very similar in both catalytic domain structure and active site arrangement to the pseudouridine synthases RsuA, TruB, and TruA. We identify five sequence motifs, two of which are novel, in the RluA, RsuA, TruB, and TruA families, uniting them as one superfamily. These results strongly suggest that four of the five families of pseudouridine synthases arose by divergent evolution. The RluD structure also provides insight into its multisite specificity.
==About this Structure==
==About this Structure==
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1QYU 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=1QYU OCA].
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1QYU 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=1QYU OCA].
==Reference==
==Reference==
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Crystal structure of the catalytic domain of RluD, the only rRNA pseudouridine synthase required for normal growth of Escherichia coli., del Campo M, Ofengand J, Malhotra A, RNA. 2004 Feb;10(2):231-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14730022 14730022]
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Crystal structure of the catalytic domain of RluD, the only rRNA pseudouridine synthase required for normal growth of Escherichia coli., Del Campo M, Ofengand J, Malhotra A, RNA. 2004 Feb;10(2):231-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14730022 14730022]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Pseudouridylate synthase]]
[[Category: Pseudouridylate synthase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Campo, M.Del.]]
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[[Category: Campo, M Del.]]
[[Category: Malhotra, A.]]
[[Category: Malhotra, A.]]
[[Category: Ofengand, J.]]
[[Category: Ofengand, J.]]
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[[Category: rlud]]
[[Category: rlud]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:08:01 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:45:15 2008''

Revision as of 12:45, 21 February 2008


1qyu, resolution 2.00Å

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Structure of the catalytic domain of 23S rRNA pseudouridine synthase RluD

Overview

Escherichia coli pseudouridine synthase RluD makes pseudouridines 1911, 1915, and 1917 in the loop of helix 69 in 23S RNA. These are the most highly conserved ribosomal pseudouridines known. Of 11 pseudouridine synthases in E. coli, only cells lacking RluD have severe growth defects and abnormal ribosomes. We have determined the 2.0 A structure of the catalytic domain of RluD (residues 77-326), the first structure of an RluA family member. The catalytic domain folds into a mainly antiparallel beta-sheet flanked by several loops and helices. A positively charged cleft that presumably binds RNA leads to the conserved Asp 139. The RluD N-terminal S4 domain, connected by a flexible linker, is disordered in our structure. RluD is very similar in both catalytic domain structure and active site arrangement to the pseudouridine synthases RsuA, TruB, and TruA. We identify five sequence motifs, two of which are novel, in the RluA, RsuA, TruB, and TruA families, uniting them as one superfamily. These results strongly suggest that four of the five families of pseudouridine synthases arose by divergent evolution. The RluD structure also provides insight into its multisite specificity.

About this Structure

1QYU 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

Crystal structure of the catalytic domain of RluD, the only rRNA pseudouridine synthase required for normal growth of Escherichia coli., Del Campo M, Ofengand J, Malhotra A, RNA. 2004 Feb;10(2):231-9. PMID:14730022

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