1n0y
From Proteopedia
(New page: 200px<br /><applet load="1n0y" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n0y, resolution 1.75Å" /> '''Crystal Structure of...) |
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| - | [[Image:1n0y.jpg|left|200px]]<br /><applet load="1n0y" size=" | + | [[Image:1n0y.jpg|left|200px]]<br /><applet load="1n0y" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1n0y, resolution 1.75Å" /> | caption="1n0y, resolution 1.75Å" /> | ||
'''Crystal Structure of Pb-bound Calmodulin'''<br /> | '''Crystal Structure of Pb-bound Calmodulin'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Calmodulin (CaM) regulates a variety of cellular processes by interacting | + | Calmodulin (CaM) regulates a variety of cellular processes by interacting with a large number of proteins in a Ca(2+)-dependent manner. Conformational flexibility plays a key role in CaM function, although the full extent and detailed features of this flexibility are not fully characterized. Here, the 1.75 A resolution crystal structure of Pb(2+)-bound Paramecium tetraurelia CaM crystallized in a previously unobserved monoclinic lattice is reported. Pb(2+)-CaM is disordered in this new lattice and only a portion of each of the two molecules in the asymmetric unit can be modeled. Comparison of the structures of Ca(2+)-CaM and Pb(2+)-CaM show close agreement in the C-terminal domain but significant structural differences in the N-terminal domain. In addition, translation-libration-screw (TLS) refinement and Rosenfield difference analysis reveal inter-helical flexibility in the metal-bound N-terminal domain of the protein that is absent in the metal-bound C-terminal domain and indicates that the two structurally similar domains of CaM are dynamically distinct. These results demonstrate that TLS refinement and Rosenfield difference analysis allow detailed information about macromolecular flexibility to be extracted from X-ray diffraction data even when the crystal lattice prohibits full manifestation of this flexibility. |
==About this Structure== | ==About this Structure== | ||
| - | 1N0Y is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Paramecium_tetraurelia Paramecium tetraurelia] with PB, CAC and ACT as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1N0Y is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Paramecium_tetraurelia Paramecium tetraurelia] with <scene name='pdbligand=PB:'>PB</scene>, <scene name='pdbligand=CAC:'>CAC</scene> and <scene name='pdbligand=ACT:'>ACT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N0Y OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Paramecium tetraurelia]] | [[Category: Paramecium tetraurelia]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Brunger, A | + | [[Category: Brunger, A T.]] |
| - | [[Category: Wilson, M | + | [[Category: Wilson, M A.]] |
[[Category: ACT]] | [[Category: ACT]] | ||
[[Category: CAC]] | [[Category: CAC]] | ||
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[[Category: lead]] | [[Category: lead]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:01:03 2008'' |
Revision as of 12:01, 21 February 2008
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Crystal Structure of Pb-bound Calmodulin
Overview
Calmodulin (CaM) regulates a variety of cellular processes by interacting with a large number of proteins in a Ca(2+)-dependent manner. Conformational flexibility plays a key role in CaM function, although the full extent and detailed features of this flexibility are not fully characterized. Here, the 1.75 A resolution crystal structure of Pb(2+)-bound Paramecium tetraurelia CaM crystallized in a previously unobserved monoclinic lattice is reported. Pb(2+)-CaM is disordered in this new lattice and only a portion of each of the two molecules in the asymmetric unit can be modeled. Comparison of the structures of Ca(2+)-CaM and Pb(2+)-CaM show close agreement in the C-terminal domain but significant structural differences in the N-terminal domain. In addition, translation-libration-screw (TLS) refinement and Rosenfield difference analysis reveal inter-helical flexibility in the metal-bound N-terminal domain of the protein that is absent in the metal-bound C-terminal domain and indicates that the two structurally similar domains of CaM are dynamically distinct. These results demonstrate that TLS refinement and Rosenfield difference analysis allow detailed information about macromolecular flexibility to be extracted from X-ray diffraction data even when the crystal lattice prohibits full manifestation of this flexibility.
About this Structure
1N0Y is a Single protein structure of sequence from Paramecium tetraurelia with , and as ligands. Full crystallographic information is available from OCA.
Reference
Domain flexibility in the 1.75 A resolution structure of Pb2+-calmodulin., Wilson MA, Brunger AT, Acta Crystallogr D Biol Crystallogr. 2003 Oct;59(Pt 10):1782-92. Epub 2003, Sep 19. PMID:14501118
Page seeded by OCA on Thu Feb 21 14:01:03 2008
Categories: Paramecium tetraurelia | Single protein | Brunger, A T. | Wilson, M A. | ACT | CAC | PB | Calmodulin | Lead
