1ssb: Difference between revisions
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==A STRUCTURAL INVESTIGATION OF CATALYTICALLY MODIFIED F12OL AND F12OY SEMISYNTHETIC RIBONUCLEASES== | ==A STRUCTURAL INVESTIGATION OF CATALYTICALLY MODIFIED F12OL AND F12OY SEMISYNTHETIC RIBONUCLEASES== | ||
<StructureSection load='1ssb' size='340' side='right' caption='[[1ssb]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='1ssb' size='340' side='right' caption='[[1ssb]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
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<table><tr><td colspan='2'>[[1ssb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SSB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SSB FirstGlance]. <br> | <table><tr><td colspan='2'>[[1ssb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SSB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SSB FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ssb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ssb OCA], [http://pdbe.org/1ssb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ssb RCSB], [http://www.ebi.ac.uk/pdbsum/1ssb PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ssb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ssb OCA], [http://pdbe.org/1ssb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ssb RCSB], [http://www.ebi.ac.uk/pdbsum/1ssb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ssb ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ss/1ssb_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ss/1ssb_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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==See Also== | ==See Also== | ||
*[[Ribonuclease|Ribonuclease]] | *[[Ribonuclease|Ribonuclease]] | ||
*[[Temp|Temp]] | *[[Temp|Temp]] | ||
== References == | == References == | ||
Revision as of 11:08, 14 March 2018
A STRUCTURAL INVESTIGATION OF CATALYTICALLY MODIFIED F12OL AND F12OY SEMISYNTHETIC RIBONUCLEASESA STRUCTURAL INVESTIGATION OF CATALYTICALLY MODIFIED F12OL AND F12OY SEMISYNTHETIC RIBONUCLEASES
Structural highlights
Function[RNAS1_BOVIN] Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single stranded and double stranded RNA.[1] 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 PubMedThe structures of two catalytically modified semisynthetic RNases obtained by replacing phenylalanine 120 with leucine and tyrosine have been determined and refined at a resolution of 2.0 A (R = 0.161 and 0.184, respectively). These structures have been compared with the refined 1.8-A structure (R = 0.204) of the fully active phenylalanine-containing enzyme (Martin PD, Doscher MS, Edwards BFP, 1987, J Biol Chem 262:15930-15938) and with the catalytically defective D121A (2.0 A, R = 0.172) and D121N (2.0 A, R = 0.186) analogs (deMel VSJ, Martin PD, Doscher MS, Edwards BFP, 1992, J Biol Chem 267:247-256). The movement away from the active site of the loop containing residues 65-72 is seen in all three catalytically defective analogs--F120L, D121A, and D121N--but not in the fully active (or hyperactive) F120Y. The insertion of the phenolic hydroxyl of Tyr 120 into a hydrogen-bonding network involving the hydroxyl group of Ser 123 and a water molecule in F120Y is the likely basis for the hyperactivity toward uridine 2',3'-cyclic phosphate previously found for this analog (Hodges RS, Merrifield RB, 1974, Int J Pept Protein Res 6:397-405) as well as the threefold increase in KM for cytidine 2',3'-cyclic phosphate found for this analog by ourselves. Structural investigation of catalytically modified F120L and F120Y semisynthetic ribonucleases.,deMel VS, Doscher MS, Glinn MA, Martin PD, Ram ML, Edwards BF Protein Sci. 1994 Jan;3(1):39-50. PMID:8142897[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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