1n0y

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[[Image:1n0y.jpg|left|200px]]
[[Image:1n0y.jpg|left|200px]]
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{{Structure
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|PDB= 1n0y |SIZE=350|CAPTION= <scene name='initialview01'>1n0y</scene>, resolution 1.75&Aring;
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The line below this paragraph, containing "STRUCTURE_1n0y", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=PB:LEAD+(II)+ION'>PB</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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|GENE= CAM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5888 Paramecium tetraurelia])
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|DOMAIN=
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{{STRUCTURE_1n0y| PDB=1n0y | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1n0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n0y OCA], [http://www.ebi.ac.uk/pdbsum/1n0y PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1n0y RCSB]</span>
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'''Crystal Structure of Pb-bound Calmodulin'''
'''Crystal Structure of Pb-bound Calmodulin'''
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[[Category: Brunger, A T.]]
[[Category: Brunger, A T.]]
[[Category: Wilson, M A.]]
[[Category: Wilson, M A.]]
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[[Category: calmodulin]]
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[[Category: Calmodulin]]
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[[Category: lead]]
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[[Category: Lead]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:57:07 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:23:51 2008''
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Revision as of 22:57, 2 May 2008

Image:1n0y.jpg

Template:STRUCTURE 1n0y

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. 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 Sat May 3 01:57:07 2008

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