This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.




1m2a

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1m2a.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1m2a.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1m2a| PDB=1m2a | SCENE= }}
{{STRUCTURE_1m2a| PDB=1m2a | SCENE= }}
-
'''Crystal structure at 1.5 Angstroms resolution of the wild type thioredoxin-like [2Fe-2S] ferredoxin from Aquifex aeolicus'''
+
===Crystal structure at 1.5 Angstroms resolution of the wild type thioredoxin-like [2Fe-2S] ferredoxin from Aquifex aeolicus===
-
==Overview==
+
<!--
-
The [2Fe-2S] ferredoxin (Fd4) from Aquifex aeolicus adopts a thioredoxin-like polypeptide fold that is distinct from other [2Fe-2S] ferredoxins. Crystal structures of the Cys-55 --&gt; Ser (C55S) and Cys-59 --&gt; Ser (C59S) variants of this protein have been determined to 1.25 A and 1.05 A resolution, respectively, whereas the resolution of the wild type (WT) has been extended to 1.5 A. The improved WT structure provides a detailed description of the [2Fe-2S] cluster, including two features that have not been noted previously in any [2Fe-2S] cluster-containing protein, namely, pronounced distortions in the cysteine coordination to the cluster and a Calpha-H-Sgamma hydrogen bond between cluster ligands Cys-55 and Cys-9. These features may contribute to the unusual electronic and magnetic properties of the [2Fe-2S] clusters in WT and variants of this ferredoxin. The structures of the two variants of Fd4, in which single cysteine ligands to the [2Fe-2S] cluster are replaced by serine, establish the metric details of serine-ligated Fe-S active sites with unprecedented accuracy. Both the cluster and its surrounding protein matrix change in subtle ways to accommodate this ligand substitution, particularly in terms of distortions of the Fe(2)S(2) inorganic core from planarity and displacements of the polypeptide chain. These high resolution structures illustrate how the interactions between polypeptide chains and Fe-S active sites reflect combinations of flexibility and rigidity on the part of both partners; these themes are also evident in more complex systems, as exemplified by changes associated with serine ligation of the nitrogenase P cluster.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12089152}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12089152 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12089152}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Ferredoxin]]
[[Category: Ferredoxin]]
[[Category: Thioredoxin-like fold]]
[[Category: Thioredoxin-like fold]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:32:53 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 23:03:59 2008''

Revision as of 20:04, 2 July 2008

Image:1m2a.png

Template:STRUCTURE 1m2a

Crystal structure at 1.5 Angstroms resolution of the wild type thioredoxin-like [2Fe-2S] ferredoxin from Aquifex aeolicus

Template:ABSTRACT PUBMED 12089152

About this Structure

1M2A is a Single protein structure of sequence from Aquifex aeolicus. Full crystallographic information is available from OCA.

Reference

High resolution crystal structures of the wild type and Cys-55-->Ser and Cys-59-->Ser variants of the thioredoxin-like [2Fe-2S] ferredoxin from Aquifex aeolicus., Yeh AP, Ambroggio XI, Andrade SL, Einsle O, Chatelet C, Meyer J, Rees DC, J Biol Chem. 2002 Sep 13;277(37):34499-507. Epub 2002 Jun 27. PMID:12089152

Page seeded by OCA on Wed Jul 2 23:03:59 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1m2a"
Personal tools