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[[Image:1jvv.jpg|left|200px]]
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{{STRUCTURE_1jvv|  PDB=1jvv  |  SCENE=  }}
'''CRYSTAL STRUCTURE OF RIBONUCLEASE A (RETRO-SOAKED FORM)'''


==CRYSTAL STRUCTURE OF RIBONUCLEASE A (RETRO-SOAKED FORM)==
<StructureSection load='1jvv' size='340' side='right'caption='[[1jvv]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1jvv]] 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=1JVV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JVV 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]] 2.2&#8491;</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=1jvv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jvv OCA], [https://pdbe.org/1jvv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jvv RCSB], [https://www.ebi.ac.uk/pdbsum/1jvv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jvv 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/jv/1jvv_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=1jvv ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Despite the increasing number of successful determinations of complex protein structures the understanding of their dynamics properties is still rather limited. Using X-ray crystallography, we demonstrate that ribonuclease A (RNase A) undergoes significant domain motions upon ligand binding. In particular, when cytidine 2'-monophosphate binds to RNase A, the structure of the enzyme becomes more compact. Interestingly, our data also show that these structural alterations are fully reversible in the crystal state. These findings provide structural bases for the dynamic behavior of RNase A in the binding of the substrate shown by Petsko and coworkers (Rasmussen et al. Nature 1992;357:423-424). These subtle domain motions may assume functional relevance for more complex system and may play a significant role in the cooperativity of oligomeric enzymes.


==Overview==
Reversible substrate-induced domain motions in ribonuclease A.,Vitagliano L, Merlino A, Zagari A, Mazzarella L Proteins. 2002 Jan 1;46(1):97-104. PMID:11746706<ref>PMID:11746706</ref>
Despite the increasing number of successful determinations of complex protein structures the understanding of their dynamics properties is still rather limited. Using X-ray crystallography, we demonstrate that ribonuclease A (RNase A) undergoes significant domain motions upon ligand binding. In particular, when cytidine 2'-monophosphate binds to RNase A, the structure of the enzyme becomes more compact. Interestingly, our data also show that these structural alterations are fully reversible in the crystal state. These findings provide structural bases for the dynamic behavior of RNase A in the binding of the substrate shown by Petsko and coworkers (Rasmussen et al. Nature 1992;357:423-424). These subtle domain motions may assume functional relevance for more complex system and may play a significant role in the cooperativity of oligomeric enzymes.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1JVV 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=1JVV OCA].
</div>
<div class="pdbe-citations 1jvv" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Reversible substrate-induced domain motions in ribonuclease A., Vitagliano L, Merlino A, Zagari A, Mazzarella L, Proteins. 2002 Jan 1;46(1):97-104. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11746706 11746706]
*[[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: Mazzarella L]]
[[Category: Mazzarella, L.]]
[[Category: Merlino A]]
[[Category: Merlino, A.]]
[[Category: Vitagliano L]]
[[Category: Vitagliano, L.]]
[[Category: Zagari A]]
[[Category: Zagari, A.]]
[[Category: Protein dynamic]]
[[Category: Protein structure-function]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 21:59:20 2008''

Latest revision as of 07:39, 17 October 2024

CRYSTAL STRUCTURE OF RIBONUCLEASE A (RETRO-SOAKED FORM)CRYSTAL STRUCTURE OF RIBONUCLEASE A (RETRO-SOAKED FORM)

Structural highlights

1jvv is a 2 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 PubMed

Despite the increasing number of successful determinations of complex protein structures the understanding of their dynamics properties is still rather limited. Using X-ray crystallography, we demonstrate that ribonuclease A (RNase A) undergoes significant domain motions upon ligand binding. In particular, when cytidine 2'-monophosphate binds to RNase A, the structure of the enzyme becomes more compact. Interestingly, our data also show that these structural alterations are fully reversible in the crystal state. These findings provide structural bases for the dynamic behavior of RNase A in the binding of the substrate shown by Petsko and coworkers (Rasmussen et al. Nature 1992;357:423-424). These subtle domain motions may assume functional relevance for more complex system and may play a significant role in the cooperativity of oligomeric enzymes.

Reversible substrate-induced domain motions in ribonuclease A.,Vitagliano L, Merlino A, Zagari A, Mazzarella L Proteins. 2002 Jan 1;46(1):97-104. PMID:11746706[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. delCardayre SB, Ribo M, Yokel EM, Quirk DJ, Rutter WJ, Raines RT. Engineering ribonuclease A: production, purification and characterization of wild-type enzyme and mutants at Gln11. Protein Eng. 1995 Mar;8(3):261-73. PMID:7479688
  2. Vitagliano L, Merlino A, Zagari A, Mazzarella L. Reversible substrate-induced domain motions in ribonuclease A. Proteins. 2002 Jan 1;46(1):97-104. PMID:11746706

1jvv, resolution 2.20Å

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