1vio: Difference between revisions
New page: left|200px<br /><applet load="1vio" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vio, resolution 1.59Å" /> '''Crystal structure of... |
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[[Image:1vio.gif|left|200px]]<br /><applet load="1vio" size=" | [[Image:1vio.gif|left|200px]]<br /><applet load="1vio" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1vio, resolution 1.59Å" /> | caption="1vio, resolution 1.59Å" /> | ||
'''Crystal structure of pseudouridylate synthase'''<br /> | '''Crystal structure of pseudouridylate synthase'''<br /> | ||
==Overview== | ==Overview== | ||
The structure of the pseudouridine synthase RsuA from Haemophilus | 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. | ||
==About this Structure== | ==About this Structure== | ||
1VIO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae] with BU1 as [http://en.wikipedia.org/wiki/ligand ligand]. 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:// | 1VIO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae] with <scene name='pdbligand=BU1:'>BU1</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1VIO OCA]. | ||
==Reference== | ==Reference== | ||
Structure of the pseudouridine synthase RsuA from Haemophilus influenzae., Matte A, Louie GV, Sivaraman J, Cygler M, Burley SK, Acta | 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://ispc.weizmann.ac.il//pmbin/getpm?pmid=16511038 16511038] | ||
[[Category: Haemophilus influenzae]] | [[Category: Haemophilus influenzae]] | ||
[[Category: Pseudouridylate synthase]] | [[Category: Pseudouridylate synthase]] | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:35:42 2008'' | ||
Revision as of 16:35, 21 February 2008
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Crystal structure of pseudouridylate synthase
OverviewOverview
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.
About this StructureAbout this Structure
1VIO is a Single protein structure of sequence from Haemophilus influenzae with as ligand. Active as Pseudouridylate synthase, with EC number 4.2.1.70 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
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