2rbi
From Proteopedia
(Difference between revisions)
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<StructureSection load='2rbi' size='340' side='right'caption='[[2rbi]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='2rbi' size='340' side='right'caption='[[2rbi]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2rbi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2rbi]] is a 2 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=2RBI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RBI 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]] 2.2Å</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=2rbi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rbi OCA], [https://pdbe.org/2rbi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rbi RCSB], [https://www.ebi.ac.uk/pdbsum/2rbi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rbi ProSAT]</span></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=2rbi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rbi OCA], [https://pdbe.org/2rbi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rbi RCSB], [https://www.ebi.ac.uk/pdbsum/2rbi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rbi ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/RN_BACIN RN_BACIN] This is a purine-specific ribonuclease. | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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=2rbi ConSurf]. | </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=2rbi ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Members of the microbial guanyl-specific ribonuclease family catalyse the endonucleolytic cleavage of single-stranded RNA in a two-step reaction involving transesterification to form a 2',3'-cyclic phosphate and its subsequent hydrolysis to yield the respective 3'-phosphate. The extracellular ribonuclease from Bacillus intermedius (binase, RNase Bi) shares a common mechanism for RNA hydrolysis with mammalian RNases. Two catalytic residues in the active site of binase, Glu72 and His101, are thought to be involved in general acid-general base catalysis of RNA cleavage. Using site-directed mutagenesis, binase mutants were produced containing amino acid substitutions H101N and H101T and their catalytic properties towards RNA, poly(I), poly(A), GpC and guanosine 2',3'-cyclic phosphate (cGMP) substrates were studied. The engineered mutant proteins are active in the transesterification step which produces the 2',3'-cyclic phosphate species but they have lost the ability to catalyse hydrolysis of the cyclic phosphate to give the 3' monophosphate product. | ||
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| - | RNA cleavage without hydrolysis. Splitting the catalytic activities of binase with Asn101 and Thr101 mutations.,Okorokov AL, Panov KI, Offen WA, Mukhortov VG, Antson AA, Karpeisky MYa, Wilkinson AJ, Dodson GG Protein Eng. 1997 Mar;10(3):273-8. PMID:9153077<ref>PMID:9153077</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2rbi" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Ribonuclease 3D structures|Ribonuclease 3D structures]] | *[[Ribonuclease 3D structures|Ribonuclease 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bacillus intermedius]] | [[Category: Bacillus intermedius]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Offen | + | [[Category: Offen WA]] |
| - | [[Category: Okorokov | + | [[Category: Okorokov AL]] |
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Current revision
STRUCTURE OF BINASE MUTANT HIS 101 ASN
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