1r5c

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[[Image:1r5c.jpg|left|200px]]<br /><applet load="1r5c" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1r5c.jpg|left|200px]]
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caption="1r5c, resolution 2.1&Aring;" />
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'''X-ray structure of the complex of Bovine seminal ribonuclease swapping dimer with d(CpA)'''<br />
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{{Structure
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|PDB= 1r5c |SIZE=350|CAPTION= <scene name='initialview01'>1r5c</scene>, resolution 2.1&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CPA:2'-DEOXYCYTIDINE-2'-DEOXYADENOSINE-3',5'-MONOPHOSPHATE'>CPA</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''X-ray structure of the complex of Bovine seminal ribonuclease swapping dimer with d(CpA)'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1R5C 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 <scene name='pdbligand=CPA:'>CPA</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=1R5C OCA].
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1R5C 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=1R5C OCA].
==Reference==
==Reference==
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Population shift vs induced fit: the case of bovine seminal ribonuclease swapping dimer., Merlino A, Vitagliano L, Sica F, Zagari A, Mazzarella L, Biopolymers. 2004 Apr 15;73(6):689-95. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15048772 15048772]
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Population shift vs induced fit: the case of bovine seminal ribonuclease swapping dimer., Merlino A, Vitagliano L, Sica F, Zagari A, Mazzarella L, Biopolymers. 2004 Apr 15;73(6):689-95. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15048772 15048772]
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Pancreatic ribonuclease]]
[[Category: Pancreatic ribonuclease]]
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[[Category: ligand binding]]
[[Category: ligand binding]]
[[Category: population shift]]
[[Category: population shift]]
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[[Category: protein dynamics]]
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[[Category: protein dynamic]]
[[Category: protein structure-function]]
[[Category: protein structure-function]]
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[[Category: ribonucleases]]
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[[Category: ribonuclease]]
[[Category: x-ray diffraction]]
[[Category: x-ray diffraction]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:47:19 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:47:03 2008''

Revision as of 11:47, 20 March 2008


PDB ID 1r5c

Drag the structure with the mouse to rotate
, resolution 2.1Å
Ligands:
Activity: Pancreatic ribonuclease, with EC number 3.1.27.5
Coordinates: save as pdb, mmCIF, xml



X-ray structure of the complex of Bovine seminal ribonuclease swapping dimer with d(CpA)


Overview

Bovine seminal ribonuclease (BS-RNase) is a unique member of the pancreatic-like ribonuclease superfamily. This enzyme exists as two conformational isomers with distinctive biological properties. The structure of the major isomer is characterized by the swapping of the N-terminal segment (MxM BS-RNase). In this article, the crystal structures of the ligand-free MxM BS-RNase and its complex with 2'-deoxycitidylyl(3',5')-2'-deoxyadenosine derived from isomorphous crystals have been refined. Interestingly, the comparison between this novel ligand-free form and the previously published sulfate-bound structure reveals significant differences. In particular, the ligand-free MxM BS-RNase is closer to the structure of MxM BS-RNase productive complexes than to the sulfate-bound form. These results reveal that MxM BS-RNase presents a remarkable flexibility, despite the structural constraints of the interchain disulfide bridges and the swapping of the N-terminal helices. These findings have important implications to the ligand binding mechanism of MxM BS-RNase. Indeed, a population shift rather than a substrate-induced conformational transition may occur in the MxM BS-RNase ligand binding process.

About this Structure

1R5C is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

Population shift vs induced fit: the case of bovine seminal ribonuclease swapping dimer., Merlino A, Vitagliano L, Sica F, Zagari A, Mazzarella L, Biopolymers. 2004 Apr 15;73(6):689-95. PMID:15048772

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