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[[Image:4bir.gif|left|200px]]<br /><applet load="4bir" size="350" color="white" frame="true" align="right" spinBox="true"
caption="4bir, resolution 1.70&Aring;" />
'''RIBONUCLEASE T1: FREE HIS92GLN MUTANT'''<br />


==Overview==
==RIBONUCLEASE T1: FREE HIS92GLN MUTANT==
Histidine-40 is known to participate in phosphodiester transesterification, catalyzed by the enzyme ribonuclease T1. A mutant enzyme with a lysine, replacing the histidine-40 (His40Lys RNase T1) retains considerable, catalytic activity [Steyaert, J., Hallenga, K., Wyns, L., &amp; Stanssens, P., (1990) Biochemistry 29, 9064-9072]. We report on the crystal structures of, His40Lys RNase T1 containing a phosphate anion and a guanosine, 2'-phosphate inhibitor in the active site, respectively. Similar to, previously described structures, the phosphate-containing crystals are of, space group P2(1)2(1)2(1), with one molecule per asymmetric unit (a =, 48.27 A, b = 46.50 A, c = 41.14 A). The complex with 2'-GMP crystallized, in the lower symmetry space group P2(1), with two molecules per asymmetric, unit (a = 49.20 A, b = 48.19 A, c = 40.16 A, beta = 90.26). The crystal, structures have been solved at 1.8- and 2.0-A resolution yielding R values, of 14.5% and 16.0%, respectively. Comparison of these His40Lys structures, with the corresponding wild-type structures, containing 2'-GMP [Arni, R., Heinemann, U., Tokuoka, R., &amp; Saenger, W. (1988) J. Biol. Chem. 263, 15358-15368] and vanadate [Kostrewa, D., Hui-Woog Choe, Heinemann, U., &amp;, Saenger, W. (1989) Biochemistry 28, 7692-7600] in the active site, respectively, leads to the following conclusions. First, the His40Lys, mutation causes no significant changes in the overall structure of RNase, T1; second, the Lys40 side chains in the mutant structures occupy roughly, the same space as His40 in the corresponding wild-type RNase T1, structures.(ABSTRACT TRUNCATED AT 250 WORDS)
<StructureSection load='4bir' size='340' side='right'caption='[[4bir]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4bir]] 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=4BIR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BIR 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]] 1.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=4bir FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bir OCA], [https://pdbe.org/4bir PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bir RCSB], [https://www.ebi.ac.uk/pdbsum/4bir PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bir 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/bi/4bir_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=4bir ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Histidine-40 is known to participate in phosphodiester transesterification catalyzed by the enzyme ribonuclease T1. A mutant enzyme with a lysine replacing the histidine-40 (His40Lys RNase T1) retains considerable catalytic activity [Steyaert, J., Hallenga, K., Wyns, L., &amp; Stanssens, P. (1990) Biochemistry 29, 9064-9072]. We report on the crystal structures of His40Lys RNase T1 containing a phosphate anion and a guanosine 2'-phosphate inhibitor in the active site, respectively. Similar to previously described structures, the phosphate-containing crystals are of space group P2(1)2(1)2(1), with one molecule per asymmetric unit (a = 48.27 A, b = 46.50 A, c = 41.14 A). The complex with 2'-GMP crystallized in the lower symmetry space group P2(1), with two molecules per asymmetric unit (a = 49.20 A, b = 48.19 A, c = 40.16 A, beta = 90.26). The crystal structures have been solved at 1.8- and 2.0-A resolution yielding R values of 14.5% and 16.0%, respectively. Comparison of these His40Lys structures with the corresponding wild-type structures, containing 2'-GMP [Arni, R., Heinemann, U., Tokuoka, R., &amp; Saenger, W. (1988) J. Biol. Chem. 263, 15358-15368] and vanadate [Kostrewa, D., Hui-Woog Choe, Heinemann, U., &amp; Saenger, W. (1989) Biochemistry 28, 7692-7600] in the active site, respectively, leads to the following conclusions. First, the His40Lys mutation causes no significant changes in the overall structure of RNase T1; second, the Lys40 side chains in the mutant structures occupy roughly the same space as His40 in the corresponding wild-type RNase T1 structures.(ABSTRACT TRUNCATED AT 250 WORDS)


==About this Structure==
Role of histidine-40 in ribonuclease T1 catalysis: three-dimensionalstructures of the partially active His40Lys mutant.,Zegers I, Verhelst P, Choe HW, Steyaert J, Heinemann U, Saenger W, Wyns L Biochemistry. 1992 Nov 24;31(46):11317-25. PMID:1445870<ref>PMID:1445870</ref>
4BIR 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 <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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] Known structural/functional Site: <scene name='pdbsite=CAT:Catalytic+Site'>CAT</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BIR OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Role of histidine-40 in ribonuclease T1 catalysis: three-dimensionalstructures of the partially active His40Lys mutant., Zegers I, Verhelst P, Choe HW, Steyaert J, Heinemann U, Saenger W, Wyns L, Biochemistry. 1992 Nov 24;31(46):11317-25. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1445870 1445870]
</div>
<div class="pdbe-citations 4bir" 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: Doumen J]]
[[Category: Doumen, J.]]
[[Category: Steyaert J]]
[[Category: Steyaert, J.]]
[[Category: CA]]
[[Category: endoribonuclease]]
[[Category: his to gln mutant]]
[[Category: hydrolase]]
[[Category: ribonuclease]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:52:45 2008''

Latest revision as of 13:41, 6 November 2024

RIBONUCLEASE T1: FREE HIS92GLN MUTANTRIBONUCLEASE T1: FREE HIS92GLN MUTANT

Structural highlights

4bir 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 1.7Å
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

Histidine-40 is known to participate in phosphodiester transesterification catalyzed by the enzyme ribonuclease T1. A mutant enzyme with a lysine replacing the histidine-40 (His40Lys RNase T1) retains considerable catalytic activity [Steyaert, J., Hallenga, K., Wyns, L., & Stanssens, P. (1990) Biochemistry 29, 9064-9072]. We report on the crystal structures of His40Lys RNase T1 containing a phosphate anion and a guanosine 2'-phosphate inhibitor in the active site, respectively. Similar to previously described structures, the phosphate-containing crystals are of space group P2(1)2(1)2(1), with one molecule per asymmetric unit (a = 48.27 A, b = 46.50 A, c = 41.14 A). The complex with 2'-GMP crystallized in the lower symmetry space group P2(1), with two molecules per asymmetric unit (a = 49.20 A, b = 48.19 A, c = 40.16 A, beta = 90.26). The crystal structures have been solved at 1.8- and 2.0-A resolution yielding R values of 14.5% and 16.0%, respectively. Comparison of these His40Lys structures with the corresponding wild-type structures, containing 2'-GMP [Arni, R., Heinemann, U., Tokuoka, R., & Saenger, W. (1988) J. Biol. Chem. 263, 15358-15368] and vanadate [Kostrewa, D., Hui-Woog Choe, Heinemann, U., & Saenger, W. (1989) Biochemistry 28, 7692-7600] in the active site, respectively, leads to the following conclusions. First, the His40Lys mutation causes no significant changes in the overall structure of RNase T1; second, the Lys40 side chains in the mutant structures occupy roughly the same space as His40 in the corresponding wild-type RNase T1 structures.(ABSTRACT TRUNCATED AT 250 WORDS)

Role of histidine-40 in ribonuclease T1 catalysis: three-dimensionalstructures of the partially active His40Lys mutant.,Zegers I, Verhelst P, Choe HW, Steyaert J, Heinemann U, Saenger W, Wyns L Biochemistry. 1992 Nov 24;31(46):11317-25. PMID:1445870[1]

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

See Also

References

  1. ↑ Zegers I, Verhelst P, Choe HW, Steyaert J, Heinemann U, Saenger W, Wyns L. Role of histidine-40 in ribonuclease T1 catalysis: three-dimensionalstructures of the partially active His40Lys mutant. Biochemistry. 1992 Nov 24;31(46):11317-25. PMID:1445870

4bir, resolution 1.70Å

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