1ssa: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
New page: left|200px<br /><applet load="1ssa" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ssa, resolution 2.0Å" /> '''A STRUCTURAL INVESTIG...
 
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
 
(19 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1ssa.gif|left|200px]]<br /><applet load="1ssa" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1ssa, resolution 2.0&Aring;" />
'''A STRUCTURAL INVESTIGATION OF CATALYTICALLY MODIFIED F12OL AND F12OY SEMISYNTHETIC RIBONUCLEASES'''<br />


==Overview==
==A STRUCTURAL INVESTIGATION OF CATALYTICALLY MODIFIED F12OL AND F12OY SEMISYNTHETIC RIBONUCLEASES==
The 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.
<StructureSection load='1ssa' size='340' side='right'caption='[[1ssa]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ssa]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SSA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SSA 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]] 2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=1ssa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ssa OCA], [https://pdbe.org/1ssa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ssa RCSB], [https://www.ebi.ac.uk/pdbsum/1ssa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ssa ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RNAS1_BOVIN RNAS1_BOVIN] Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single stranded and double stranded RNA.<ref>PMID:7479688</ref>
== 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/ss/1ssa_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=1ssa ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The 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.


==About this Structure==
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<ref>PMID:8142897</ref>
1SSA is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SSA OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8142897 8142897]
</div>
[[Category: Protein complex]]
<div class="pdbe-citations 1ssa" style="background-color:#fffaf0;"></div>
[[Category: Demel, V.S.J.]]
[[Category: Doscher, M.S.]]
[[Category: Edwards, B.F.P.]]
[[Category: Glinn, M.A.]]
[[Category: Martin, P.D.]]
[[Category: Ram, M.L.]]
[[Category: SO4]]
[[Category: hydrolase(endoribonuclease)]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:37:21 2007''
==See Also==
*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bos taurus]]
[[Category: Large Structures]]
[[Category: Doscher MS]]
[[Category: Edwards BFP]]
[[Category: Glinn MA]]
[[Category: Martin PD]]
[[Category: Ram ML]]
[[Category: DeMel VSJ]]
Retrieved from "https://proteopedia.org/1ssa"