4fxc

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:4fxc.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:4fxc.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_4fxc| PDB=4fxc | SCENE= }}
{{STRUCTURE_4fxc| PDB=4fxc | SCENE= }}
-
'''TERTIARY STRUCTURE OF [2FE-2S] FERREDOXIN FROM SPIRULINA PLATENSIS REFINED AT 2.5 ANGSTROMS RESOLUTION: STRUCTURAL COMPARISONS OF PLANT-TYPE FERREDOXINS AND AN ELECTROSTATIC POTENTIAL ANALYSIS'''
+
===TERTIARY STRUCTURE OF [2FE-2S] FERREDOXIN FROM SPIRULINA PLATENSIS REFINED AT 2.5 ANGSTROMS RESOLUTION: STRUCTURAL COMPARISONS OF PLANT-TYPE FERREDOXINS AND AN ELECTROSTATIC POTENTIAL ANALYSIS===
-
==Overview==
+
<!--
-
The structure of plant-type [2Fe-2S] ferredoxin isolated from Spirulina platensis has been refined using diffraction data to 2.5 A resolution by alternate cycles of simulated annealing and manual revision of the model. The final R factor is 19.9% for 2,912 reflections with F &gt; 2 sigma F between 8.0 and 2.5 A resolution. S. platensis ferredoxin, like other plant-type [2Fe-2S] ferredoxins, has a major alpha-helix flanking a sheet consisting of four beta strands. The present refinement revises the conformation of residues 56-71, in which a one-turn helix was identified. Superposition of the Spirulina ferredoxin structure on the structures of other ferredoxins that have been well refined showed structural perturbation at a few residues on the amino and carboxyl termini and the turn between the first and second beta-strands. The root-mean-square deviations of the corresponding C alpha atoms of the pairs of ferredoxins range from 0.90 to 1.17 A for all the residues, but from 0.64 to 0.70 A if the few perturbed residues are excluded. Therefore, it may be concluded that the main-chain foldings of all the plant-type [2Fe-2S] ferredoxins are essentially the same. Electrostatic potential analysis showed that the molecular surface around the cluster is negatively charged, whereas that of the beta-sheet of the other side is positively charged. The interaction between ferredoxin and ferredoxin-NADP+ reductase is discussed on the basis of the charge distributions of these molecules and biochemical data.
+
The line below this paragraph, {{ABSTRACT_PUBMED_8586613}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 8586613 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_8586613}}
==About this Structure==
==About this Structure==
Line 25: Line 29:
[[Category: Tsukihara, T.]]
[[Category: Tsukihara, T.]]
[[Category: Electron transport]]
[[Category: Electron transport]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:24:15 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 13:37:48 2008''

Revision as of 10:37, 3 July 2008

Image:4fxc.png

Template:STRUCTURE 4fxc

TERTIARY STRUCTURE OF [2FE-2S] FERREDOXIN FROM SPIRULINA PLATENSIS REFINED AT 2.5 ANGSTROMS RESOLUTION: STRUCTURAL COMPARISONS OF PLANT-TYPE FERREDOXINS AND AN ELECTROSTATIC POTENTIAL ANALYSIS

Template:ABSTRACT PUBMED 8586613

About this Structure

4FXC is a Single protein structure of sequence from Arthrospira platensis. This structure supersedes the now removed PDB entries and 1fxc. Full crystallographic information is available from OCA.

Reference

Tertiary structure of [2Fe-2S] ferredoxin from Spirulina platensis refined at 2.5 A resolution: structural comparisons of plant-type ferredoxins and an electrostatic potential analysis., Fukuyama K, Ueki N, Nakamura H, Tsukihara T, Matsubara H, J Biochem. 1995 May;117(5):1017-23. PMID:8586613

Page seeded by OCA on Thu Jul 3 13:37:48 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4fxc"
Personal tools