1n0y: Difference between revisions

Revision as of 13:49, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1n0y.png

Template:STRUCTURE 1n0y

Crystal Structure of Pb-bound CalmodulinCrystal Structure of Pb-bound Calmodulin

Template:ABSTRACT PUBMED 14501118

About this StructureAbout this Structure

1N0Y is a Single protein structure of sequence from Paramecium tetraurelia. Full crystallographic information is available from OCA.

ReferenceReference

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 Mon Jul 28 13:49:33 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1n0y.jpg|left|200px]]
+{{Seed}}
+[[Image:1n0y.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1n0y|  PDB=1n0y  |  SCENE=  }}
-'''Crystal Structure of Pb-bound Calmodulin'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_14501118}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 14501118 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_14501118}}
 ==About this Structure==
@@ Line 26: / Line 30: @@
 [[Category: Calmodulin]]
 [[Category: Lead]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 01:57:07 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:49:33 2008''