1vs3: Difference between revisions

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Crystal Structure of the tRNA Pseudouridine Synthase TruA From Thermus thermophilus HB8

OverviewOverview

The pseudouridine synthase (Psi synthase) TruA catalyzes the conversion of uridine to pseudouridine at positions 38, 39 and/or 40 in the anticodon stem-loop (ASL) of tRNA. We have determined the crystal structure of TruA from Thermus thermophilus HB8 at 2.25 A resolution. TruA and the other (Psi synthases have a completely conserved active site aspartate, which suggests that the members of this enzyme family share a common catalytic mechanism. The T. thermophilus TruA structure reveals the remarkably flexible structural features in the tRNA-binding cleft, which may be responsible for the primary tRNA interaction. In addition, the charged residues occupying the intermediate positions in the cleft may lead the tRNA to the active site for catalysis. Based on the TruB-tRNA complex structure, the T. thermophilus TruA structure reveals that the tRNA probably makes the melting base pairs move into the cleft, and suggests that a conformational change of the substrate tRNA is necessary to facilitate access to the active site aspartate residue, deep within the cleft.

About this StructureAbout this Structure

1VS3 is a Single protein structure of sequence from Thermus thermophilus. Active as tRNA-pseudouridine synthase I, with EC number 5.4.99.12 Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of tRNA pseudouridine synthase TruA from Thermus thermophilus HB8., Dong X, Bessho Y, Shibata R, Nishimoto M, Shirouzu M, Kuramitsu S, Yokoyama S, RNA Biol. 2006 Jul;3(3):115-22. Epub 2006 Jul 17. PMID:17114947

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-[[Image:1vs3.jpg|left|200px]]<br /><applet load="1vs3" size="450" color="white" frame="true" align="right" spinBox="true"
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 caption="1vs3, resolution 2.25&Aring;" />
 '''Crystal Structure of the tRNA Pseudouridine Synthase TruA From Thermus thermophilus HB8'''<br />
 ==Overview==
-The pseudouridine synthase (Psi synthase) TruA catalyzes the conversion of, uridine to pseudouridine at positions 38, 39 and/or 40 in the anticodon, stem-loop (ASL) of tRNA. We have determined the crystal structure of TruA, from Thermus thermophilus HB8 at 2.25 A resolution. TruA and the other, (Psi synthases have a completely conserved active site aspartate, which, suggests that the members of this enzyme family share a common catalytic, mechanism. The T. thermophilus TruA structure reveals the remarkably, flexible structural features in the tRNA-binding cleft, which may be, responsible for the primary tRNA interaction. In addition, the charged, residues occupying the intermediate positions in the cleft may lead the, tRNA to the active site for catalysis. Based on the TruB-tRNA complex, structure, the T. thermophilus TruA structure reveals that the tRNA, probably makes the melting base pairs move into the cleft, and suggests, that a conformational change of the substrate tRNA is necessary to, facilitate access to the active site aspartate residue, deep within the, cleft.
+The pseudouridine synthase (Psi synthase) TruA catalyzes the conversion of uridine to pseudouridine at positions 38, 39 and/or 40 in the anticodon stem-loop (ASL) of tRNA. We have determined the crystal structure of TruA from Thermus thermophilus HB8 at 2.25 A resolution. TruA and the other (Psi synthases have a completely conserved active site aspartate, which suggests that the members of this enzyme family share a common catalytic mechanism. The T. thermophilus TruA structure reveals the remarkably flexible structural features in the tRNA-binding cleft, which may be responsible for the primary tRNA interaction. In addition, the charged residues occupying the intermediate positions in the cleft may lead the tRNA to the active site for catalysis. Based on the TruB-tRNA complex structure, the T. thermophilus TruA structure reveals that the tRNA probably makes the melting base pairs move into the cleft, and suggests that a conformational change of the substrate tRNA is necessary to facilitate access to the active site aspartate residue, deep within the cleft.
 ==About this Structure==
-VS3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Active as [http://en.wikipedia.org/wiki/tRNA-pseudouridine_synthase_I tRNA-pseudouridine synthase I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.12 5.4.99.12] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1VS3 OCA].
+VS3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Active as [http://en.wikipedia.org/wiki/tRNA-pseudouridine_synthase_I tRNA-pseudouridine synthase I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.12 5.4.99.12] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VS3 OCA].
 ==Reference==
-Crystal Structure of tRNA Pseudouridine Synthase TruA from Thermus thermophilus HB8., Dong X, Bessho Y, Shibata R, Nishimoto M, Shirouzu M, Kuramitsu S, Yokoyama S, RNA Biol. 2006 Jul;3(3):115-22. Epub 2006 Jul 17. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17114947 17114947]
+Crystal structure of tRNA pseudouridine synthase TruA from Thermus thermophilus HB8., Dong X, Bessho Y, Shibata R, Nishimoto M, Shirouzu M, Kuramitsu S, Yokoyama S, RNA Biol. 2006 Jul;3(3):115-22. Epub 2006 Jul 17. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17114947 17114947]
 [[Category: Single protein]]
 [[Category: Thermus thermophilus]]
@@ Line 16: / Line 16: @@
 [[Category: Bessho, Y.]]
 [[Category: Dong, X.]]
-[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]
+[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
 [[Category: Shirouzu, M.]]
 [[Category: Yokoyama, S.]]
@@ Line 28: / Line 28: @@
 [[Category: trua]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:05:58 2007''
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