1sdy: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
Line 1: Line 1:
[[Image:1sdy.jpg|left|200px]]
{{Seed}}
[[Image:1sdy.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1sdy|  PDB=1sdy  |  SCENE=  }}  
{{STRUCTURE_1sdy|  PDB=1sdy  |  SCENE=  }}  


'''STRUCTURE SOLUTION AND MOLECULAR DYNAMICS REFINEMENT OF THE YEAST CU,ZN ENZYME SUPEROXIDE DISMUTASE'''
===STRUCTURE SOLUTION AND MOLECULAR DYNAMICS REFINEMENT OF THE YEAST CU,ZN ENZYME SUPEROXIDE DISMUTASE===




==Overview==
<!--
Cu,Zn yeast superoxide dismutase was crystallized from polyethylene glycol solutions. The crystals belong to the P2(1)2(1)2 space group, with cell dimensions a = 105.3, b = 143.0, c = 62.1 A; two dimers of Mr = 32,000 each are contained in the asymmetric unit. Diffraction data at 2.5 A resolution were collected with the image-plate system at the EMBL synchrotron radiation facility in Hamburg. The structure was determined by molecular replacement using as a search model the 'blue-green' dimer of the bovine Cu,Zn superoxide dismutase. The crystallographic refinement of the molecular replacement solution was performed by means of molecular dynamics techniques and resulted in an R factor of 0.268 for the data between 6.0 and 2.5 A. The model was subsequently subjected to conventional restrained crystallographic refinement of the coordinates and temperature factors. The current R value for the data between 6.0 and 2.5 A is 0.220. Owing to the large radius of convergence of the molecular dynamics-crystallographic refinement, the convergence of the refinement process was reached after 18.1 ps of simulation time. The geometry of the active site of the enzyme appears essentially preserved compared with the bovine superoxide dismutase. The beta-barrel structure in the yeast enzyme is closed at the upper part by an efficient hydrogen-bonding scheme.
The line below this paragraph, {{ABSTRACT_PUBMED_1772629}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 1772629 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_1772629}}


==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Pelosi, G.]]
[[Category: Pelosi, G.]]
[[Category: Rotilio, G.]]
[[Category: Rotilio, G.]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 08:35:31 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 16:24:06 2008''

Revision as of 13:24, 28 July 2008

File:1sdy.png

Template:STRUCTURE 1sdy

STRUCTURE SOLUTION AND MOLECULAR DYNAMICS REFINEMENT OF THE YEAST CU,ZN ENZYME SUPEROXIDE DISMUTASE

Template:ABSTRACT PUBMED 1772629

About this Structure

1SDY is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Structure solution and molecular dynamics refinement of the yeast Cu,Zn enzyme superoxide dismutase., Djinovic K, Gatti G, Coda A, Antolini L, Pelosi G, Desideri A, Falconi M, Marmocchi F, Rolilio G, Bolognesi M, Acta Crystallogr B. 1991 Dec 1;47 ( Pt 6):918-27. PMID:1772629

Page seeded by OCA on Mon Jul 28 16:24:06 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1sdy&oldid=706873"