1jvt

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(New page: 200px<br /><applet load="1jvt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jvt, resolution 2.05&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1jvt.gif|left|200px]]<br /><applet load="1jvt" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1jvt, resolution 2.05&Aring;" />
caption="1jvt, resolution 2.05&Aring;" />
'''CRYSTAL STRUCTURE OF RIBONUCLEASE A (LIGAND-FREE FORM)'''<br />
'''CRYSTAL STRUCTURE OF RIBONUCLEASE A (LIGAND-FREE FORM)'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1JVT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. 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=1JVT OCA].
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1JVT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. 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=1JVT OCA].
==Reference==
==Reference==
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[[Category: protein structure-function]]
[[Category: protein structure-function]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:37:04 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:27:16 2008''

Revision as of 11:27, 21 February 2008


1jvt, resolution 2.05Å

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CRYSTAL STRUCTURE OF RIBONUCLEASE A (LIGAND-FREE FORM)

Overview

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

1JVT is a Single protein structure of sequence from Bos taurus. Active as Pancreatic ribonuclease, with EC number 3.1.27.5 Full crystallographic information is available from OCA.

Reference

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

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