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[[Image:1gsp.gif|left|200px]]


{{Structure
==RIBONUCLEASE T1 COMPLEXED WITH 2',3'-CGPS, 1 DAY==
|PDB= 1gsp |SIZE=350|CAPTION= <scene name='initialview01'>1gsp</scene>, resolution 2.20&Aring;
<StructureSection load='1gsp' size='340' side='right'caption='[[1gsp]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
|SITE= <scene name='pdbsite=BI1:Site'>BI1</scene>, <scene name='pdbsite=CAL:Site'>CAL</scene> and <scene name='pdbsite=CAT:Active+Site'>CAT</scene>
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=SGP:GUANOSINE-2&#39;,3&#39;-CYCLOPHOSPHOROTHIOATE'>SGP</scene>
<table><tr><td colspan='2'>[[1gsp]] 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=1GSP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GSP FirstGlance]. <br>
|ACTIVITY= [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]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=1gsp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gsp OCA], [https://pdbe.org/1gsp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gsp RCSB], [https://www.ebi.ac.uk/pdbsum/1gsp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gsp 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/1gsp_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=1gsp 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.


'''RIBONUCLEASE T1 COMPLEXED WITH 2',3'-CGPS, 1 DAY'''
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>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1gsp" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
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.
*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
 
== References ==
==About this Structure==
<references/>
1GSP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_oryzae Aspergillus oryzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GSP OCA].
__TOC__
 
</StructureSection>
==Reference==
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://www.ncbi.nlm.nih.gov/pubmed/9546218 9546218]
[[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: CA]]
[[Category: SGP]]
[[Category: endoribonuclease]]
[[Category: hydrolase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 11:59:01 2008''

Latest revision as of 03:01, 21 November 2024

RIBONUCLEASE T1 COMPLEXED WITH 2',3'-CGPS, 1 DAYRIBONUCLEASE T1 COMPLEXED WITH 2',3'-CGPS, 1 DAY

Structural highlights

1gsp 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 2.2Å
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

1gsp, resolution 2.20Å

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