4gsp: Difference between revisions

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[[Image:4gsp.gif|left|200px]]<br />
<applet load="4gsp" size="450" color="white" frame="true" align="right" spinBox="true"
caption="4gsp, resolution 1.65&Aring;" />
'''RIBONUCLEASE T1 COMPLEXED WITH 2',3'-CGPS + 3'-GMP, 7 DAYS'''<br />


==Overview==
==RIBONUCLEASE T1 COMPLEXED WITH 2',3'-CGPS + 3'-GMP, 7 DAYS==
Here we present a time-resolved crystallographic analysis of the, hydrolysis of exo (Sp) guanosine 2',3'-cyclophosphorothioate by RNase T1., The use of a slow substrate and fast crystallization methods made it, possible to perform the study with conventional data-collection, techniques. The results support the idea that the hydrolysis reaction, proceeds through a mechanism that is the inverse of the, transesterification reaction. In addition, the structures provide an, explanation for the differential behavior of RNase T1 towards exo- and, endo-cyclic thiophosphates.
<StructureSection load='4gsp' size='340' side='right'caption='[[4gsp]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4gsp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_oryzae Aspergillus oryzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GSP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GSP 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]] 1.65&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3GP:GUANOSINE-3-MONOPHOSPHATE'>3GP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SGP:GUANOSINE-2,3-CYCLOPHOSPHOROTHIOATE'>SGP</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=4gsp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gsp OCA], [https://pdbe.org/4gsp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gsp RCSB], [https://www.ebi.ac.uk/pdbsum/4gsp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gsp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RNT1_ASPOR RNT1_ASPOR]
== 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/gs/4gsp_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=4gsp ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Here we present a time-resolved crystallographic analysis of the hydrolysis of exo (Sp) guanosine 2',3'-cyclophosphorothioate by RNase T1. The use of a slow substrate and fast crystallization methods made it possible to perform the study with conventional data-collection techniques. The results support the idea that the hydrolysis reaction proceeds through a mechanism that is the inverse of the transesterification reaction. In addition, the structures provide an explanation for the differential behavior of RNase T1 towards exo- and endo-cyclic thiophosphates.


==About this Structure==
Hydrolysis of a slow cyclic thiophosphate substrate of RNase T1 analyzed by time-resolved crystallography.,Zegers I, Loris R, Dehollander G, Fattah Haikal A, Poortmans F, Steyaert J, Wyns L Nat Struct Biol. 1998 Apr;5(4):280-3. PMID:9546218<ref>PMID:9546218</ref>
4GSP is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Aspergillus_oryzae Aspergillus oryzae]] with CA and 3GP as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Ribonuclease_T(1) Ribonuclease T(1)]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.3 3.1.27.3]]. Structure known Active Sites: BI1, CAL and CAT. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=4GSP OCA]].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Hydrolysis of a slow cyclic thiophosphate substrate of RNase T1 analyzed by time-resolved crystallography., Zegers I, Loris R, Dehollander G, Fattah Haikal A, Poortmans F, Steyaert J, Wyns L, Nat Struct Biol. 1998 Apr;5(4):280-3. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9546218 9546218]
</div>
<div class="pdbe-citations 4gsp" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Aspergillus oryzae]]
[[Category: Aspergillus oryzae]]
[[Category: Ribonuclease T(1)]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Wyns L]]
[[Category: Wyns, L.]]
[[Category: Zegers I]]
[[Category: Zegers, I.]]
[[Category: 3GP]]
[[Category: CA]]
[[Category: endoribonuclease]]
[[Category: hydrolase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 17:47:47 2007''

Latest revision as of 13:02, 30 October 2024

RIBONUCLEASE T1 COMPLEXED WITH 2',3'-CGPS + 3'-GMP, 7 DAYSRIBONUCLEASE T1 COMPLEXED WITH 2',3'-CGPS + 3'-GMP, 7 DAYS

Structural highlights

4gsp is a 1 chain structure with sequence from Aspergillus oryzae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.65Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RNT1_ASPOR

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

Here we present a time-resolved crystallographic analysis of the hydrolysis of exo (Sp) guanosine 2',3'-cyclophosphorothioate by RNase T1. The use of a slow substrate and fast crystallization methods made it possible to perform the study with conventional data-collection techniques. The results support the idea that the hydrolysis reaction proceeds through a mechanism that is the inverse of the transesterification reaction. In addition, the structures provide an explanation for the differential behavior of RNase T1 towards exo- and endo-cyclic thiophosphates.

Hydrolysis of a slow cyclic thiophosphate substrate of RNase T1 analyzed by time-resolved crystallography.,Zegers I, Loris R, Dehollander G, Fattah Haikal A, Poortmans F, Steyaert J, Wyns L Nat Struct Biol. 1998 Apr;5(4):280-3. PMID:9546218[1]

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

See Also

References

  1. Zegers I, Loris R, Dehollander G, Fattah Haikal A, Poortmans F, Steyaert J, Wyns L. Hydrolysis of a slow cyclic thiophosphate substrate of RNase T1 analyzed by time-resolved crystallography. Nat Struct Biol. 1998 Apr;5(4):280-3. PMID:9546218

4gsp, resolution 1.65Å

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