1rra
From Proteopedia
(New page: 200px<br /><applet load="1rra" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rra, resolution 2.5Å" /> '''RIBONUCLEASE A FROM R...) |
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| - | [[Image:1rra.jpg|left|200px]]<br /><applet load="1rra" size=" | + | [[Image:1rra.jpg|left|200px]]<br /><applet load="1rra" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1rra, resolution 2.5Å" /> | caption="1rra, resolution 2.5Å" /> | ||
'''RIBONUCLEASE A FROM RATTUS NORVEGICUS (COMMON RAT)'''<br /> | '''RIBONUCLEASE A FROM RATTUS NORVEGICUS (COMMON RAT)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional structure of rat pancreatic RNase A expressed in | + | The three-dimensional structure of rat pancreatic RNase A expressed in Escherichia coli was determined. The backbone conformations of certain critical loops are significantly different in this enzyme compared to its bovine counterpart. However, the core structure of rat RNase A is similar to that of the other members of the pancreatic ribonuclease family. The structural variations within a loop bordering the active site can be correlated with the subtle differences in the enzymatic activities of bovine and rat ribonucleases for different substrates. The most significant difference in the backbone conformation was observed in the loop 15-25. This loop incorporates the subtilisin cleavage site which is responsible for RNase A to RNase S conversion in the bovine enzyme. The rat enzyme does not get cleaved under identical conditions. Molecular docking of this region of the rat enzyme in the active site of subtilisin shows steric incompatibility, although the bovine pancreatic ribonuclease A appropriately fits into this active site. It is therefore inferred that the local conformation of the substrate governs the specificity of subtilisin. |
==About this Structure== | ==About this Structure== | ||
| - | 1RRA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with PO4 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:// | + | 1RRA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=PO4:'>PO4</scene> 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1RRA OCA]. |
==Reference== | ==Reference== | ||
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[[Category: ribonuclease]] | [[Category: ribonuclease]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:53:50 2008'' |
Revision as of 12:53, 21 February 2008
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RIBONUCLEASE A FROM RATTUS NORVEGICUS (COMMON RAT)
Overview
The three-dimensional structure of rat pancreatic RNase A expressed in Escherichia coli was determined. The backbone conformations of certain critical loops are significantly different in this enzyme compared to its bovine counterpart. However, the core structure of rat RNase A is similar to that of the other members of the pancreatic ribonuclease family. The structural variations within a loop bordering the active site can be correlated with the subtle differences in the enzymatic activities of bovine and rat ribonucleases for different substrates. The most significant difference in the backbone conformation was observed in the loop 15-25. This loop incorporates the subtilisin cleavage site which is responsible for RNase A to RNase S conversion in the bovine enzyme. The rat enzyme does not get cleaved under identical conditions. Molecular docking of this region of the rat enzyme in the active site of subtilisin shows steric incompatibility, although the bovine pancreatic ribonuclease A appropriately fits into this active site. It is therefore inferred that the local conformation of the substrate governs the specificity of subtilisin.
About this Structure
1RRA is a Single protein structure of sequence from Rattus norvegicus with as ligand. Active as Pancreatic ribonuclease, with EC number 3.1.27.5 Full crystallographic information is available from OCA.
Reference
The crystal structure of recombinant rat pancreatic RNase A., Gupta V, Muyldermans S, Wyns L, Salunke DM, Proteins. 1999 Apr 1;35(1):1-12. PMID:10090281
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