1ksk: Difference between revisions

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New page: left|200px<br /><applet load="1ksk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ksk, resolution 2.0Å" /> '''STRUCTURE OF RSUA'''<...
 
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[[Image:1ksk.gif|left|200px]]<br /><applet load="1ksk" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1ksk.gif|left|200px]]<br /><applet load="1ksk" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1ksk, resolution 2.0&Aring;" />
caption="1ksk, resolution 2.0&Aring;" />
'''STRUCTURE OF RSUA'''<br />
'''STRUCTURE OF RSUA'''<br />


==Overview==
==Overview==
In Escherichia coli, the pseudouridine synthase RsuA catalyzes formation, of pseudouridine (psi) at position 516 in 16S rRNA during assembly of the, 30S ribosomal subunit. We have determined the crystal structure of RsuA, bound to uracil at 2.0 A resolution and to uridine 5'-monophosphate (UMP), at 2.65 A resolution. RsuA consists of an N-terminal domain connected by, an extended linker to the central and C-terminal domains. Uracil and UMP, bind in a cleft between the central and C-terminal domains near the, catalytic residue Asp 102. The N-terminal domain shows structural, similarity to the ribosomal protein S4. Despite only 15% amino acid, identity, the other two domains are structurally similar to those of the, tRNA-specific psi-synthase TruA, including the position of the catalytic, Asp. Our results suggest that all four families of pseudouridine synthases, share the same fold of their catalytic domain(s) and uracil-binding site.
In Escherichia coli, the pseudouridine synthase RsuA catalyzes formation of pseudouridine (psi) at position 516 in 16S rRNA during assembly of the 30S ribosomal subunit. We have determined the crystal structure of RsuA bound to uracil at 2.0 A resolution and to uridine 5'-monophosphate (UMP) at 2.65 A resolution. RsuA consists of an N-terminal domain connected by an extended linker to the central and C-terminal domains. Uracil and UMP bind in a cleft between the central and C-terminal domains near the catalytic residue Asp 102. The N-terminal domain shows structural similarity to the ribosomal protein S4. Despite only 15% amino acid identity, the other two domains are structurally similar to those of the tRNA-specific psi-synthase TruA, including the position of the catalytic Asp. Our results suggest that all four families of pseudouridine synthases share the same fold of their catalytic domain(s) and uracil-binding site.


==About this Structure==
==About this Structure==
1KSK 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 URA 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KSK OCA].  
1KSK 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=URA:'>URA</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=1KSK OCA].  


==Reference==
==Reference==
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[[Category: Matte, A.]]
[[Category: Matte, A.]]
[[Category: Sauve, V.]]
[[Category: Sauve, V.]]
[[Category: Schrag, J.D.]]
[[Category: Schrag, J D.]]
[[Category: Sivaraman, J.]]
[[Category: Sivaraman, J.]]
[[Category: Stura, E.A.]]
[[Category: Stura, E A.]]
[[Category: URA]]
[[Category: URA]]
[[Category: crystal structure]]
[[Category: crystal structure]]
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[[Category: rsua]]
[[Category: rsua]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:37:28 2008''

Revision as of 14:37, 21 February 2008

File:1ksk.gif


1ksk, resolution 2.0Å

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STRUCTURE OF RSUA

OverviewOverview

In Escherichia coli, the pseudouridine synthase RsuA catalyzes formation of pseudouridine (psi) at position 516 in 16S rRNA during assembly of the 30S ribosomal subunit. We have determined the crystal structure of RsuA bound to uracil at 2.0 A resolution and to uridine 5'-monophosphate (UMP) at 2.65 A resolution. RsuA consists of an N-terminal domain connected by an extended linker to the central and C-terminal domains. Uracil and UMP bind in a cleft between the central and C-terminal domains near the catalytic residue Asp 102. The N-terminal domain shows structural similarity to the ribosomal protein S4. Despite only 15% amino acid identity, the other two domains are structurally similar to those of the tRNA-specific psi-synthase TruA, including the position of the catalytic Asp. Our results suggest that all four families of pseudouridine synthases share the same fold of their catalytic domain(s) and uracil-binding site.

About this StructureAbout this Structure

1KSK is a Single protein structure of sequence from Escherichia coli 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 16S rRNA pseudouridine synthase RsuA bound to uracil and UMP., Sivaraman J, Sauve V, Larocque R, Stura EA, Schrag JD, Cygler M, Matte A, Nat Struct Biol. 2002 May;9(5):353-8. PMID:11953756

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