1srd: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
Line 1: Line 1:
[[Image:1srd.jpg|left|200px]]
{{Seed}}
[[Image:1srd.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1srd|  PDB=1srd  |  SCENE=  }}  
{{STRUCTURE_1srd|  PDB=1srd  |  SCENE=  }}  


'''THREE-DIMENSIONAL STRUCTURE OF CU,ZN-SUPEROXIDE DISMUTASE FROM SPINACH AT 2.0 ANGSTROMS RESOLUTION'''
===THREE-DIMENSIONAL STRUCTURE OF CU,ZN-SUPEROXIDE DISMUTASE FROM SPINACH AT 2.0 ANGSTROMS RESOLUTION===




==Overview==
<!--  
The three-dimensional structure of Cu,Zn-superoxide dismutase from spinach leaves has been determined by X-ray crystal structure analysis. The atomic coordinates were refined at 2.0 A resolution using the Hendrickson and Konnert program for stereochemically restrained refinement against structure factors, which allowed the use of non-crystallographic symmetry. The crystallographic residual error for the refined model was 24.9%, with a root mean square deviation of 0.03 A from the ideal bond length and an average atomic temperature factor of 9.6 A. A dimeric molecule of the enzyme is comprised of two identical subunits related by a non-crystallographic 2-fold axis. Each subunit of 154 amino acid residues is composed primarily of eight anti-parallel beta-strands that form a flattened cylinder, plus three external loops. The main-chain hydrogen bonds primarily link the beta-strands. The overall structure of this enzyme is quite similar to that of the bovine dismutase except for some parts. The single disulfide bridge (Cys57-Cys146) and the salt bridge (Arg79-Asp101) may stabilize the loop regions of the structure. The Cu2+ and Zn2+ ions in the active site lie 6.1 A apart at the bottom of the long channel. The Cu2+ ligands (ND1 of His-46, and NE2 of His-48, -63, and -120) show an uneven tetrahedral distortion from a square plane. The Zn2+ ligands (ND1 of His-63, -71, and -80 and OD1 of Asp-83) show an almost tetrahedral geometry. The imidazole ring of His-63 forms a bridge between the Cu2+ and Zn2+ ions.(ABSTRACT TRUNCATED AT 250 WORDS)
The line below this paragraph, {{ABSTRACT_PUBMED_1880134}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 1880134 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_1880134}}


==About this Structure==
==About this Structure==
Line 25: Line 29:
[[Category: Katsube, Y.]]
[[Category: Katsube, Y.]]
[[Category: Kitagawa, Y.]]
[[Category: Kitagawa, Y.]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 09:03:33 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 02:14:54 2008''

Revision as of 23:15, 27 July 2008

File:1srd.png

Template:STRUCTURE 1srd

THREE-DIMENSIONAL STRUCTURE OF CU,ZN-SUPEROXIDE DISMUTASE FROM SPINACH AT 2.0 ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 1880134

About this Structure

1SRD is a Single protein structure of sequence from Spinacia oleracea. Full crystallographic information is available from OCA.

Reference

Three-dimensional structure of Cu,Zn-superoxide dismutase from spinach at 2.0 A resolution., Kitagawa Y, Tanaka N, Hata Y, Kusunoki M, Lee GP, Katsube Y, Asada K, Aibara S, Morita Y, J Biochem. 1991 Mar;109(3):477-85. PMID:1880134

Page seeded by OCA on Mon Jul 28 02:14:54 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1srd&oldid=676203"