1xso: Difference between revisions

Revision as of 13:07, 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:1xso.png

Template:STRUCTURE 1xso

THREE-DIMENSIONAL STRUCTURE OF XENOPUS LAEVIS CU,ZN SUPEROXIDE DISMUTASE B DETERMINED BY X-RAY CRYSTALLOGRAPHY AT 1.5 ANGSTROMS RESOLUTIONTHREE-DIMENSIONAL STRUCTURE OF XENOPUS LAEVIS CU,ZN SUPEROXIDE DISMUTASE B DETERMINED BY X-RAY CRYSTALLOGRAPHY AT 1.5 ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 15299740

About this StructureAbout this Structure

1XSO is a Single protein structure of sequence from Xenopus laevis. Full crystallographic information is available from OCA.

ReferenceReference

Three-dimensional structure of Xenopus laevis Cu,Zn superoxide dismutase b determined by X-ray crystallography at 1.5 A resolution., Djinovic Carugo K, Battistoni A, Carri MT, Polticelli F, Desideri A, Rotilio G, Coda A, Wilson KS, Bolognesi M, Acta Crystallogr D Biol Crystallogr. 1996 Jan 1;52(Pt 1):176-88. PMID:15299740

Page seeded by OCA on Mon Jul 28 13:07:36 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1xso.jpg|left|200px]]
+{{Seed}}
+[[Image:1xso.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1xso|  PDB=1xso  |  SCENE=  }}
-'''THREE-DIMENSIONAL STRUCTURE OF XENOPUS LAEVIS CU,ZN SUPEROXIDE DISMUTASE B DETERMINED BY X-RAY CRYSTALLOGRAPHY AT 1.5 ANGSTROMS RESOLUTION'''
+===THREE-DIMENSIONAL STRUCTURE OF XENOPUS LAEVIS CU,ZN SUPEROXIDE DISMUTASE B DETERMINED BY X-RAY CRYSTALLOGRAPHY AT 1.5 ANGSTROMS RESOLUTION===
-==Overview==
+<!--
-Xenopus laevis Cu,Zn superoxide dismutase (recombinant isoenzyme b) has been crystallized and the structure determined at 1.49 A resolution. The crystals belong to space group P2(1)2(1)2(1), with cell constants a = 73.33, b = 68.86, c = 59.73 A, and contain one dimeric molecule of M(r) 32 000 per asymmetric unit. The structure was solved by molecular-replacement techniques using the semisynthetic Cu,Co bovine enzyme as search model, and refined by molecular dynamics with a crystallographic pseudo-energy term. During the final steps, positional and anisotropic thermal parameters of the atoms were refined. The R factor for the 49 209 unique reflections in the 10.0-1.49 A resolution range is 0.104, for a model comprising 2023 protein atoms, two Cu(2+), two Zn(2+), and 353 water molecules. The overall temperature factor for the model, including solvent, is 20.3 A(2), while the calculated r.m.s. coordinate error for the refined model is 0.036 A. As suggested by the primary structure homology to any other known intracellular eukaryotic superoxide dismutase (&gt; 50%), the typical structural scaffolding of flattened antiparallel eight-stranded (beta-barrel is well conserved in X. laevis Cu,Zn superoxide dismutase b, together with the coordination geometry of the metal centers in the active site. The higher thermal stability of the bb X. laevis superoxide dismutase homodimer, with respect to dimers involving the a-type isoenzyme subunit(s), can be related, on the basis of the high-resolution structure, to side-chain and solvent interactions centered on residue Tyr149, in both b-type subunits. The analysis of the overall solvent structure reveals a number of equivalent water molecule sites in the two subunits, and in homologous superoxide dismutase models. Their locations are discussed in detail and classified on the basis of their structural role.
+The line below this paragraph, {{ABSTRACT_PUBMED_15299740}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15299740 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15299740}}
 ==About this Structure==
@@ Line 32: / Line 36: @@
 [[Category: Rotilio, G.]]
 [[Category: Wilson, K S.]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 15:27:48 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:07:36 2008''