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3lwv

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Structure of H/ACA RNP bound to a substrate RNA containing 2'-deoxyuridine

Structural highlights

3lwv is a 5 chain structure with sequence from Atcc 43587. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Related:	3lwo, 3lwp, 3lwq, 3lwr
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[TRUB_PYRFU] Could be responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs (By similarity). [RL7A_PYRFU] Multifunctional RNA-binding protein that recognizes the K-turn motif in ribosomal RNA, box H/ACA, box C/D and box C'/D' sRNAs (By similarity). [NOP10_PYRFU] Involved in ribosome biogenesis; more specifically in 18S rRNA pseudouridylation and in cleavage of pre-rRNA (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Box H/ACA ribonucleoprotein protein particles catalyze the majority of pseudouridylation in functional RNA. Different from stand alone pseudouridine synthases, the RNP pseudouridine synthase comprises multiple protein subunits and an RNA subunit. Previous studies showed that each subunit, regardless its location, is sensitive to the step of subunit placement at the catalytic center and potentially to the reaction status of the substrate. Here we describe the impact of chemical substitutions of target uridine on enzyme activity and structure. We found that 3-methyluridine in place of uridine inhibited its isomerization while 2'-deoxyuridine or 4-thiouridine did not. Significantly, crystal structures of an archaeal box H/ACA RNP bound with the nonreactive and the two postreactive substrate analogues showed only subtle structural changes throughout the assembly except for a conserved tyrosine and a substrate anchoring loop of Cbf5. Our results suggest a potential role of these elements and the subunit that contacts them in substrate binding and product release.

Functional and Structural Impact of Target Uridine Substitutions on the H/ACA Ribonucleoprotein Particle Pseudouridine Synthase .,Zhou J, Liang B, Li H Biochemistry. 2010 Jul 2. PMID:20575532^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Zhou J, Liang B, Li H. Functional and Structural Impact of Target Uridine Substitutions on the H/ACA Ribonucleoprotein Particle Pseudouridine Synthase . Biochemistry. 2010 Jul 2. PMID:20575532 doi:10.1021/bi1006699

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3lwv"

@@ Line 1: / Line 1: @@
 ==Structure of H/ACA RNP bound to a substrate RNA containing 2'-deoxyuridine==
-<StructureSection load='3lwv' size='340' side='right' caption='[[3lwv]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
+<StructureSection load='3lwv' size='340' side='right'caption='[[3lwv]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3lwv]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43587 Atcc 43587]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LWV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LWV FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3lwv]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43587 Atcc 43587]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LWV OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3LWV FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=DU:2-DEOXYURIDINE-5-MONOPHOSPHATE'>DU</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3lwo|3lwo]], [[3lwp|3lwp]], [[3lwq|3lwq]], [[3lwr|3lwr]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3lwv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lwv OCA], [http://pdbe.org/3lwv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3lwv RCSB], [http://www.ebi.ac.uk/pdbsum/3lwv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3lwv ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3lwv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lwv OCA], [http://pdbe.org/3lwv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3lwv RCSB], [http://www.ebi.ac.uk/pdbsum/3lwv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3lwv ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 33: / Line 33: @@
 ==See Also==
 *[[Guide-independent Pseudouridine synthase|Guide-independent Pseudouridine synthase]]
+*[[Pseudouridine synthase 3D structures|Pseudouridine synthase 3D structures]]
 *[[Ribosome biogenesis protein|Ribosome biogenesis protein]]
 == References ==
@@ Line 39: / Line 40: @@
 </StructureSection>
 [[Category: Atcc 43587]]
+[[Category: Large Structures]]
 [[Category: Li, H]]
 [[Category: Liang, B]]

3lwv

From Proteopedia

Current revision

Structure of H/ACA RNP bound to a substrate RNA containing 2'-deoxyuridine

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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