2oxi: 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:2oxi.gif|left|200px]]
{{Seed}}
[[Image:2oxi.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2oxi|  PDB=2oxi  |  SCENE=  }}  
{{STRUCTURE_2oxi|  PDB=2oxi  |  SCENE=  }}  


'''REFINED CRYSTAL STRUCTURE OF CU-SUBSTITUTED ALCOHOL DEHYDROGENASE AT 2.1 ANGSTROMS RESOLUTION'''
===REFINED CRYSTAL STRUCTURE OF CU-SUBSTITUTED ALCOHOL DEHYDROGENASE AT 2.1 ANGSTROMS RESOLUTION===




==Overview==
<!--  
Liver alcohol dehydrogenase (LADH) is a Zn(II)-dependent dimeric enzyme. LADH with the active-site Zn(II) substituted by Cu(II) resembles blue (type I) copper proteins by its spectroscopic characteristics. In this work we present the X-ray structure of the active site Cu(II)-substituted LADH complex with NADH and dimethyl sulfoxide (DMSO). The structure was solved by molecular replacement. The space group is P2(1) with cell dimensions a = 44.4, b = 180.6, c = 50.8 A and beta = 108 degrees. There is one dimer of the enzyme in the asymmetric unit. The refinement was carried out to a crystallographic R-factor of 16.1% for 41 119 unique reflections in the resolution range 12.0 to 2.1 A. The coordination geometry of Cu(II) in LADH is compared with the active-site metal coordination in the Zn-LADH-NADH-DMSO complex and blue-copper proteins. The distances from the metal to the protein ligands (Cys46, His67 and Cys174) are similar for the Zn(II) and Cu(II) ions. The distances of the O atom of the inhibitor DMSO to the Cu(II) ion in the two subunits of the dimer are 3.19 and 3.45 A. These are considerably longer than the corresponding distances for the Zn(II) enzyme, 2.19 and 2.15 A. The Cu(II) ion is positioned nearly in the plane of the three protein ligands (NS(2)) with a geometry similar to the trigonal arrangement of the three strongly bound ligands (N(2)S) in blue-copper proteins. This coordination probably accounts for the similarity of the spectral characteristics of Cu(II)-LADH and type I copper proteins.
The line below this paragraph, {{ABSTRACT_PUBMED_15299812}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 15299812 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_15299812}}


==About this Structure==
==About this Structure==
Line 25: Line 29:
[[Category: Al-Karadaghi, S.]]
[[Category: Al-Karadaghi, S.]]
[[Category: Cedergren-Zeppezauer, E S.]]
[[Category: Cedergren-Zeppezauer, E S.]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 11:52:41 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 16:16:25 2008''

Revision as of 13:16, 29 July 2008

File:2oxi.png

Template:STRUCTURE 2oxi

REFINED CRYSTAL STRUCTURE OF CU-SUBSTITUTED ALCOHOL DEHYDROGENASE AT 2.1 ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 15299812

About this Structure

2OXI is a Single protein structure of sequence from Equus caballus. Full crystallographic information is available from OCA.

Reference

Refined structure of Cu-substituted alcohol dehydrogenase at 2.1 A resolution., Al-Karadaghi S, Cedergren-Zeppezauer ES, Dauter Z, Wilson KS, Acta Crystallogr D Biol Crystallogr. 1995 Sep 1;51(Pt 5):805-13. PMID:15299812

Page seeded by OCA on Tue Jul 29 16:16:25 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=2oxi&oldid=748652"