1m5p: Difference between revisions

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New page: left|200px<br /> <applet load="1m5p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m5p, resolution 2.60Å" /> '''Transition State St...
 
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[[Image:1m5p.gif|left|200px]]<br />
<applet load="1m5p" size="450" color="white" frame="true" align="right" spinBox="true"
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'''Transition State Stabilization by a Catalytic RNA'''<br />


==Overview==
==Transition State Stabilization by a Catalytic RNA==
The hairpin ribozyme catalyzes sequence-specific cleavage of RNA through, transesterification of the scissile phosphate. Vanadate has previously, been used as a transition state mimic of protein enzymes that catalyze the, same reaction. Comparison of the 2.2 angstrom resolution structure of a, vanadate-hairpin ribozyme complex with structures of precursor and product, complexes reveals a rigid active site that makes more hydrogen bonds to, the transition state than to the precursor or product. Because of the, paucity of RNA functional groups capable of general acid-base or, electrostatic catalysis, transition state stabilization is likely to be an, important catalytic strategy for ribozymes.
<StructureSection load='1m5p' size='340' side='right'caption='[[1m5p]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1m5p]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M5P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M5P FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5CG:5-CHLORO-5-DEOXY-GUANOSINE'>5CG</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1m5p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m5p OCA], [https://pdbe.org/1m5p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m5p RCSB], [https://www.ebi.ac.uk/pdbsum/1m5p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m5p ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SNRPA_HUMAN SNRPA_HUMAN] Binds stem loop II of U1 snRNA. It is the first snRNP to interact with pre-mRNA. This interaction is required for the subsequent binding of U2 snRNP and the U4/U6/U5 tri-snRNP. In a snRNP-free form (SF-A) may be involved in coupled pre-mRNA splicing and polyadenylation process. Binds preferentially to the 5'-UGCAC-3' motif in vitro.<ref>PMID:9848648</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m5/1m5p_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1m5p ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1M5P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M5P OCA].
*[[Nucleoprotein 3D structures|Nucleoprotein 3D structures]]
 
*[[Ribozyme 3D structures|Ribozyme 3D structures]]
==Reference==
== References ==
Transition state stabilization by a catalytic RNA., Rupert PB, Massey AP, Sigurdsson ST, Ferre-D'Amare AR, Science. 2002 Nov 15;298(5597):1421-4. Epub 2002 Oct 10. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12376595 12376595]
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Amare, A.R.Ferre-D.]]
[[Category: Ferre-D'Amare AR]]
[[Category: Massey, A.]]
[[Category: Massey A]]
[[Category: Rupert, P.B.]]
[[Category: Rupert PB]]
[[Category: Sigurdsson, S.T.]]
[[Category: Sigurdsson ST]]
[[Category: CA]]
[[Category: catalytic rna]]
[[Category: cl5*]]
[[Category: hairpin ribozyme]]
[[Category: u1a rna binding protein]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:07:48 2007''

Latest revision as of 10:40, 14 February 2024

Transition State Stabilization by a Catalytic RNATransition State Stabilization by a Catalytic RNA

Structural highlights

1m5p is a 8 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.6Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SNRPA_HUMAN Binds stem loop II of U1 snRNA. It is the first snRNP to interact with pre-mRNA. This interaction is required for the subsequent binding of U2 snRNP and the U4/U6/U5 tri-snRNP. In a snRNP-free form (SF-A) may be involved in coupled pre-mRNA splicing and polyadenylation process. Binds preferentially to the 5'-UGCAC-3' motif in vitro.[1]

Evolutionary Conservation

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

See Also

References

  1. Lutz CS, Cooke C, O'Connor JP, Kobayashi R, Alwine JC. The snRNP-free U1A (SF-A) complex(es): identification of the largest subunit as PSF, the polypyrimidine-tract binding protein-associated splicing factor. RNA. 1998 Dec;4(12):1493-9. PMID:9848648

1m5p, resolution 2.60Å

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