1vio: Difference between revisions

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[[Image:1vio.gif|left|200px]]
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[[Image:1vio.png|left|200px]]


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{{STRUCTURE_1vio|  PDB=1vio  |  SCENE=  }}  
{{STRUCTURE_1vio|  PDB=1vio  |  SCENE=  }}  


'''Crystal structure of pseudouridylate synthase'''
===Crystal structure of pseudouridylate synthase===




==Overview==
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The structure of the pseudouridine synthase RsuA from Haemophilus influenza, which catalyzes the conversion of uridine to pseudouridine at a single position within 16S ribosomal RNA, has been determined at 1.59 A resolution and compared with that of Escherichia coli RsuA. The H. influenza enzyme contains an N-terminal S4-like alpha3beta4 domain followed by a catalytic domain, as observed in the structure of E. coli RsuA. Whereas the individual domains of E. coli and H. influenza RsuA are structurally similar, their relative spatial disposition differs greatly between the two structures. The former displays an extended open conformation with no direct contacts between the domains, while the latter is in a closed conformation with a large interface between the two domains. Domain closure presents several basic and polar residues into a putative RNA-binding cleft. It is proposed that this relative repositioning of the S4 and catalytic domains is used to modulate the shape and size of the rRNA-binding site in RsuA and in other pseudouridine synthases possessing S4 domains.
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{{ABSTRACT_PUBMED_16511038}}


==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Structure of the pseudouridine synthase RsuA from Haemophilus influenzae., Matte A, Louie GV, Sivaraman J, Cygler M, Burley SK, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Apr 1;61(Pt, 4):350-4. Epub 2005 Mar 12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16511038 16511038]
Structure of the pseudouridine synthase RsuA from Haemophilus influenzae., Matte A, Louie GV, Sivaraman J, Cygler M, Burley SK, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Apr 1;61(Pt, 4):350-4. Epub 2005 Mar 12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16511038 16511038]
Structural analysis of a set of proteins resulting from a bacterial genomics project., Badger J, Sauder JM, Adams JM, Antonysamy S, Bain K, Bergseid MG, Buchanan SG, Buchanan MD, Batiyenko Y, Christopher JA, Emtage S, Eroshkina A, Feil I, Furlong EB, Gajiwala KS, Gao X, He D, Hendle J, Huber A, Hoda K, Kearins P, Kissinger C, Laubert B, Lewis HA, Lin J, Loomis K, Lorimer D, Louie G, Maletic M, Marsh CD, Miller I, Molinari J, Muller-Dieckmann HJ, Newman JM, Noland BW, Pagarigan B, Park F, Peat TS, Post KW, Radojicic S, Ramos A, Romero R, Rutter ME, Sanderson WE, Schwinn KD, Tresser J, Winhoven J, Wright TA, Wu L, Xu J, Harris TJ, Proteins. 2005 Sep 1;60(4):787-96. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16021622 16021622]
[[Category: Haemophilus influenzae]]
[[Category: Haemophilus influenzae]]
[[Category: Pseudouridylate synthase]]
[[Category: Pseudouridylate synthase]]
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[[Category: GenomiX, Structural.]]
[[Category: GenomiX, Structural.]]
[[Category: Structural genomic]]
[[Category: Structural genomic]]
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Revision as of 00:21, 29 July 2008

File:1vio.png

Template:STRUCTURE 1vio

Crystal structure of pseudouridylate synthaseCrystal structure of pseudouridylate synthase

Template:ABSTRACT PUBMED 16511038

About this StructureAbout this Structure

1VIO is a Single protein structure of sequence from Haemophilus influenzae. Full crystallographic information is available from OCA.

ReferenceReference

Structure of the pseudouridine synthase RsuA from Haemophilus influenzae., Matte A, Louie GV, Sivaraman J, Cygler M, Burley SK, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Apr 1;61(Pt, 4):350-4. Epub 2005 Mar 12. PMID:16511038

Structural analysis of a set of proteins resulting from a bacterial genomics project., Badger J, Sauder JM, Adams JM, Antonysamy S, Bain K, Bergseid MG, Buchanan SG, Buchanan MD, Batiyenko Y, Christopher JA, Emtage S, Eroshkina A, Feil I, Furlong EB, Gajiwala KS, Gao X, He D, Hendle J, Huber A, Hoda K, Kearins P, Kissinger C, Laubert B, Lewis HA, Lin J, Loomis K, Lorimer D, Louie G, Maletic M, Marsh CD, Miller I, Molinari J, Muller-Dieckmann HJ, Newman JM, Noland BW, Pagarigan B, Park F, Peat TS, Post KW, Radojicic S, Ramos A, Romero R, Rutter ME, Sanderson WE, Schwinn KD, Tresser J, Winhoven J, Wright TA, Wu L, Xu J, Harris TJ, Proteins. 2005 Sep 1;60(4):787-96. PMID:16021622

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