1rnv

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1rnv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rnv, resolution 1.6&Aring;" /> '''REFINEMENT OF THE CRY...)
Current revision (04:51, 17 October 2024) (edit) (undo)
 
(17 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1rnv.gif|left|200px]]<br /><applet load="1rnv" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1rnv, resolution 1.6&Aring;" />
 
-
'''REFINEMENT OF THE CRYSTAL STRUCTURE OF RIBONUCLEASE S. COMPARISON WITH AND BETWEEN THE VARIOUS RIBONUCLEASE A STRUCTURES'''<br />
 
-
==Overview==
+
==REFINEMENT OF THE CRYSTAL STRUCTURE OF RIBONUCLEASE S. COMPARISON WITH AND BETWEEN THE VARIOUS RIBONUCLEASE A STRUCTURES==
-
Ribonuclease S (RNase-S) is a complex that consists of two proteolytic, fragments of bovine pancreatic ribonuclease A (RNase-A): the S-peptide, (residues 1-20) and S-protein (residues 21-124). We have refined the, crystal structures of three RNase-S complexes. The first two contain the, full-length 20-residue S-peptide and were studied at pHs of 4.75 and 5.5., The third one consists of a truncated form of S-peptide (residues 1-15), and was studied at pH 4.75 as the reference structure for a series of, mutant peptide complexes to be reported separately. Excluding residues, 16-23 which are either missing (in the S15 complex) or disordered (in both, S20 complexes), all three structures refined at 1.6-A resolution are, identical within the estimated errors in the coordinates (0.048 A for the, backbone atoms). The R-values, residual error, range from 17.4% to 18.6%., The final model of S20, pH 4.75, includes 1 sulfate and 84 water, molecules. The side chains of 11 residues were modeled in two discrete, conformations. The final structures were independent of the particular, RNase-A or RNase-S used as a starting model. An extensive comparison with, refined crystal structures of RNase-A reveals that the core of the, molecule which is held together with extensive hydrogen bonds is in, identical pattern in all cases. However, the loop regions vary from one, structure to another and are often characterized by high B-factors. The, pattern of thermal parameters appears to be dependent on crystal packing, and correlates well with the accessibility calculated in the crystal., Gln60 is a conserved residue in all sequences known to date for this class, of ribonucleases. However, it is the only residue that is clearly defined, in an unfavorable position (phi = -100 degrees, psi = -130 degrees) on the, Ramachandran plot. The origin of the substantial differences between, RNase-A and RNase-S in stability to both acid and temperature denaturation, and in susceptibility to proteolysis at neutral pH is not obvious in our, visual comparison of these two structures.
+
<StructureSection load='1rnv' size='340' side='right'caption='[[1rnv]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1rnv]] is a 1 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=1RNV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RNV 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]] 1.6&#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=1rnv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rnv OCA], [https://pdbe.org/1rnv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rnv RCSB], [https://www.ebi.ac.uk/pdbsum/1rnv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rnv 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/rn/1rnv_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=1rnv ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Ribonuclease S (RNase-S) is a complex that consists of two proteolytic fragments of bovine pancreatic ribonuclease A (RNase-A): the S-peptide (residues 1-20) and S-protein (residues 21-124). We have refined the crystal structures of three RNase-S complexes. The first two contain the full-length 20-residue S-peptide and were studied at pHs of 4.75 and 5.5. The third one consists of a truncated form of S-peptide (residues 1-15) and was studied at pH 4.75 as the reference structure for a series of mutant peptide complexes to be reported separately. Excluding residues 16-23 which are either missing (in the S15 complex) or disordered (in both S20 complexes), all three structures refined at 1.6-A resolution are identical within the estimated errors in the coordinates (0.048 A for the backbone atoms). The R-values, residual error, range from 17.4% to 18.6%. The final model of S20, pH 4.75, includes 1 sulfate and 84 water molecules. The side chains of 11 residues were modeled in two discrete conformations. The final structures were independent of the particular RNase-A or RNase-S used as a starting model. An extensive comparison with refined crystal structures of RNase-A reveals that the core of the molecule which is held together with extensive hydrogen bonds is in identical pattern in all cases. However, the loop regions vary from one structure to another and are often characterized by high B-factors. The pattern of thermal parameters appears to be dependent on crystal packing and correlates well with the accessibility calculated in the crystal. Gln60 is a conserved residue in all sequences known to date for this class of ribonucleases. However, it is the only residue that is clearly defined in an unfavorable position (phi = -100 degrees, psi = -130 degrees) on the Ramachandran plot. The origin of the substantial differences between RNase-A and RNase-S in stability to both acid and temperature denaturation and in susceptibility to proteolysis at neutral pH is not obvious in our visual comparison of these two structures.
-
==About this Structure==
+
Refinement of the crystal structure of ribonuclease S. Comparison with and between the various ribonuclease A structures.,Kim EE, Varadarajan R, Wyckoff HW, Richards FM Biochemistry. 1992 Dec 15;31(49):12304-14. PMID:1463719<ref>PMID:1463719</ref>
-
1RNV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Pancreatic_ribonuclease Pancreatic ribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.5 3.1.27.5] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RNV OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
Refinement of the crystal structure of ribonuclease S. Comparison with and between the various ribonuclease A structures., Kim EE, Varadarajan R, Wyckoff HW, Richards FM, Biochemistry. 1992 Dec 15;31(49):12304-14. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1463719 1463719]
+
</div>
-
[[Category: Bos taurus]]
+
<div class="pdbe-citations 1rnv" style="background-color:#fffaf0;"></div>
-
[[Category: Pancreatic ribonuclease]]
+
-
[[Category: Single protein]]
+
-
[[Category: Kim, E.E.]]
+
-
[[Category: Richards, F.M.]]
+
-
[[Category: Varadarajan, R.]]
+
-
[[Category: Wyckoff, H.W.]]
+
-
[[Category: SO4]]
+
-
[[Category: hydrolase(phosphoric diester]]
+
-
[[Category: rna)]]
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:44:26 2007''
+
==See Also==
 +
*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Bos taurus]]
 +
[[Category: Large Structures]]
 +
[[Category: Kim EE]]
 +
[[Category: Richards FM]]
 +
[[Category: Varadarajan R]]
 +
[[Category: Wyckoff HW]]

Current revision

REFINEMENT OF THE CRYSTAL STRUCTURE OF RIBONUCLEASE S. COMPARISON WITH AND BETWEEN THE VARIOUS RIBONUCLEASE A STRUCTURES

PDB ID 1rnv

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools