4haa: Difference between revisions
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==Structure of Ribonuclease Binase Glu43Ala/Phe81Ala Mutant== | ==Structure of Ribonuclease Binase Glu43Ala/Phe81Ala Mutant== | ||
<StructureSection load='4haa' size='340' side='right' caption='[[4haa]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='4haa' size='340' side='right'caption='[[4haa]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4haa]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4haa]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_intermedius Bacillus intermedius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HAA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HAA FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4haa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4haa OCA], [https://pdbe.org/4haa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4haa RCSB], [https://www.ebi.ac.uk/pdbsum/4haa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4haa ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/RN_BACIN RN_BACIN] This is a purine-specific ribonuclease. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[Ribonuclease|Ribonuclease | *[[Ribonuclease 3D structures|Ribonuclease 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Bacillus intermedius]] | [[Category: Bacillus intermedius]] | ||
[[Category: Dorovatovskii | [[Category: Large Structures]] | ||
[[Category: Goncharuk | [[Category: Dorovatovskii PV]] | ||
[[Category: Makarov | [[Category: Goncharuk DA]] | ||
[[Category: Mitchevich | [[Category: Makarov AA]] | ||
[[Category: Polyakov | [[Category: Mitchevich VA]] | ||
[[Category: Schulga | [[Category: Polyakov KM]] | ||
[[Category: Tkach | [[Category: Schulga AA]] | ||
[[Category: Trofimov | [[Category: Tkach EN]] | ||
[[Category: Trofimov AA]] | |||
Latest revision as of 18:02, 20 September 2023
Structure of Ribonuclease Binase Glu43Ala/Phe81Ala MutantStructure of Ribonuclease Binase Glu43Ala/Phe81Ala Mutant
Structural highlights
FunctionRN_BACIN This is a purine-specific ribonuclease. Publication Abstract from PubMedRibonuclease from Bacillus intermedius (binase) is a small basic protein with antitumour activity. The three-dimensional structure of the binase mutant form Glu43Ala/Phe81Ala was determined at 1.98 A resolution and its functional properties, such as the kinetic parameters characterizing the hydrolysis of polyinosinic acid and cytotoxicity towards Kasumi-1 cells, were investigated. In all crystal structures of binase studied previously the characteristic dimer is present, with the active site of one subunit being blocked owing to interactions within the dimer. In contrast to this, the new mutant form is not dimeric in the crystal. The catalytic efficiency of the mutant form is increased 1.7-fold and its cytotoxic properties are enhanced compared with the wild-type enzyme. Structure and functional studies of the ribonuclease binase Glu43Ala/Phe81Ala mutant.,Mitkevich VA, Schulga AA, Trofimov AA, Dorovatovskii PV, Goncharuk DA, Tkach EN, Makarov AA, Polyakov KM Acta Crystallogr D Biol Crystallogr. 2013 Jun;69(Pt 6):991-6. doi:, 10.1107/S0907444913004046. Epub 2013 May 11. PMID:23695243[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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