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[[Image:1rsm.gif|left|200px]]
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{{STRUCTURE_1rsm|  PDB=1rsm  |  SCENE=  }}
'''THE 2-ANGSTROMS RESOLUTION STRUCTURE OF A THERMOSTABLE RIBONUCLEASE A CHEMICALLY CROSS-LINKED BETWEEN LYSINE RESIDUES 7 AND 41'''


==THE 2-ANGSTROMS RESOLUTION STRUCTURE OF A THERMOSTABLE RIBONUCLEASE A CHEMICALLY CROSS-LINKED BETWEEN LYSINE RESIDUES 7 AND 41==
<StructureSection load='1rsm' size='340' side='right'caption='[[1rsm]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1rsm]] 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=1RSM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RSM 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=NIN:DINITROPHENYLENE'>NIN</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=1rsm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rsm OCA], [https://pdbe.org/1rsm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rsm RCSB], [https://www.ebi.ac.uk/pdbsum/1rsm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rsm 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/rs/1rsm_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=1rsm ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of Lys-7-(dinitrophenylene)-Lys-41-cross-linked ribonuclease A has been determined by molecular replacement and refined by restrained least-squares methods to an R factor of 0.18 at 2.0-A resolution. Diffraction intensity data were collected by using a conventional diffractometer and an x-ray area detector. Comparison of the thermostable cross-linked protein and the native enzyme shows them to be structurally similar, with a rms difference in backbone and side-chain atoms of 0.52 and 1.34 A, respectively. Native and modified proteins additionally show 35 common bound solvent sites and similar overall temperature factor behavior, despite localized differences resulting from cross-link introduction, altered crystal pH, or lattice interactions with neighboring molecules. These results are discussed in the context of proposals on the origins of thermostability in the cross-linked enzyme.


==Overview==
The 2-A resolution structure of a thermostable ribonuclease A chemically cross-linked between lysine residues 7 and 41.,Weber PC, Sheriff S, Ohlendorf DH, Finzel BC, Salemme FR Proc Natl Acad Sci U S A. 1985 Dec;82(24):8473-7. PMID:3936036<ref>PMID:3936036</ref>
The crystal structure of Lys-7-(dinitrophenylene)-Lys-41-cross-linked ribonuclease A has been determined by molecular replacement and refined by restrained least-squares methods to an R factor of 0.18 at 2.0-A resolution. Diffraction intensity data were collected by using a conventional diffractometer and an x-ray area detector. Comparison of the thermostable cross-linked protein and the native enzyme shows them to be structurally similar, with a rms difference in backbone and side-chain atoms of 0.52 and 1.34 A, respectively. Native and modified proteins additionally show 35 common bound solvent sites and similar overall temperature factor behavior, despite localized differences resulting from cross-link introduction, altered crystal pH, or lattice interactions with neighboring molecules. These results are discussed in the context of proposals on the origins of thermostability in the cross-linked enzyme.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1RSM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RSM OCA].
</div>
<div class="pdbe-citations 1rsm" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
The 2-A resolution structure of a thermostable ribonuclease A chemically cross-linked between lysine residues 7 and 41., Weber PC, Sheriff S, Ohlendorf DH, Finzel BC, Salemme FR, Proc Natl Acad Sci U S A. 1985 Dec;82(24):8473-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/3936036 3936036]
*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Pancreatic ribonuclease]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Finzel BC]]
[[Category: Finzel, B C.]]
[[Category: Ohlendorf DH]]
[[Category: Ohlendorf, D H.]]
[[Category: Salemme FR]]
[[Category: Salemme, F R.]]
[[Category: Sheriff S]]
[[Category: Sheriff, S.]]
[[Category: Weber PC]]
[[Category: Weber, P C.]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 07:51:32 2008''

Latest revision as of 08:47, 6 November 2024

THE 2-ANGSTROMS RESOLUTION STRUCTURE OF A THERMOSTABLE RIBONUCLEASE A CHEMICALLY CROSS-LINKED BETWEEN LYSINE RESIDUES 7 AND 41

1rsm, resolution 2.00Å

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