1m2b

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Revision as of 07:44, 31 January 2018

Crystal structure at 1.25 Angstroms resolution of the Cys55Ser variant of the thioredoxin-like [2Fe-2S] ferredoxin from Aquifex aeolicus

Structural highlights

1m2b is a 2 chain structure with sequence from "aquifex_aeolicus"_huber_and_stetter_2001 "aquifex aeolicus" huber and stetter 2001. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1f37, 1m2a, 1m2d
Gene:	Fdx4 ("Aquifex aeolicus" Huber and Stetter 2001)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[FER2_AQUAE] Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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 --> Ser (C55S) and Cys-59 --> 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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Yeh AP, Ambroggio XI, Andrade SL, Einsle O, Chatelet C, Meyer J, Rees DC. 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. J Biol Chem. 2002 Sep 13;277(37):34499-507. Epub 2002 Jun 27. PMID:12089152 doi:10.1074/jbc.M205096200

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1m2b"

@@ Line 1: / Line 1: @@
 ==Crystal structure at 1.25 Angstroms resolution of the Cys55Ser variant of the thioredoxin-like [2Fe-2S] ferredoxin from Aquifex aeolicus==
 <StructureSection load='1m2b' size='340' side='right' caption='[[1m2b]], [[Resolution|resolution]] 1.25&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1f37|1f37]], [[1m2a|1m2a]], [[1m2d|1m2d]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Fdx4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=63363 "Aquifex aeolicus" Huber and Stetter 2001])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1m2b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m2b OCA], [http://pdbe.org/1m2b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1m2b RCSB], [http://www.ebi.ac.uk/pdbsum/1m2b PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1m2b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m2b OCA], [http://pdbe.org/1m2b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1m2b RCSB], [http://www.ebi.ac.uk/pdbsum/1m2b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1m2b ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m2/1m2b_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m2/1m2b_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 29: / Line 30: @@
 </div>
 <div class="pdbe-citations 1m2b" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Ferredoxin|Ferredoxin]]
 == References ==
 <references/>

1m2b

From Proteopedia

Revision as of 07:44, 31 January 2018

Crystal structure at 1.25 Angstroms resolution of the Cys55Ser variant of the thioredoxin-like [2Fe-2S] ferredoxin from Aquifex aeolicus

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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