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.

3kx9

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 07:09, 2 January 2019

Engineering a closed form of the Archaeoglobus fulgidus ferritin by site directed mutagenesis

Structural highlights

3kx9 is a 24 chain structure with sequence from Arcfl. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1s3q, 1sq3
Gene:	AF0834, AF_0834 (ARCFL)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

Archaeoglobus fulgidus ferritin (AfFtn) is the only tetracosameric ferritin known to form a tetrahedral cage, a structure that remains unique in structural biology. As a result of the tetrahedral (2-3) symmetry, four openings ( approximately 45 A in diameter) are formed in the cage. This open tetrahedral assembly contradicts the paradigm of a typical ferritin cage: a closed assembly having octahedral (4-3-2) symmetry. To investigate the molecular mechanism affecting this atypical assembly, amino acid residues Lys-150 and Arg-151 were replaced by alanine. The data presented here shed light on the role that these residues play in shaping the unique structural features and biophysical properties of the AfFtn. The x-ray crystal structure of the K150A/R151A mutant, solved at 2.1 A resolution, indicates that replacement of these key residues flips a "symmetry switch." The engineered molecule no longer assembles with tetrahedral symmetry but forms a typical closed octahedral ferritin cage. Small angle x-ray scattering reveals that the overall shape and size of AfFtn and AfFtn-AA in solution are consistent with those observed in their respective crystal structures. Iron binding and release kinetics of the AfFtn and AfFtn-AA were investigated to assess the contribution of cage openings to the kinetics of iron oxidation, mineralization, or reductive iron release. Identical iron binding kinetics for AfFtn and AfFtn-AA suggest that Fe(2+) ions do not utilize the triangular pores for access to the catalytic site. In contrast, relatively slow reductive iron release was observed for the closed AfFtn-AA, demonstrating involvement of the large pores in the pathway for iron release.

The role of nonconserved residues of Archaeoglobus fulgidus ferritin on its unique structure and biophysical properties.,Sana B, Johnson E, Le Magueres P, Criswell A, Cascio D, Lim S J Biol Chem. 2013 Nov 8;288(45):32663-72. doi: 10.1074/jbc.M113.491191. Epub 2013, Sep 12. PMID:24030827^[1]

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

References

↑ Sana B, Johnson E, Le Magueres P, Criswell A, Cascio D, Lim S. The role of nonconserved residues of Archaeoglobus fulgidus ferritin on its unique structure and biophysical properties. J Biol Chem. 2013 Nov 8;288(45):32663-72. doi: 10.1074/jbc.M113.491191. Epub 2013, Sep 12. PMID:24030827 doi:http://dx.doi.org/10.1074/jbc.M113.491191

1 Structural highlights
2 Publication Abstract from PubMed
3 See Also
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3kx9"

@@ Line 1: / Line 1: @@
 ==Engineering a closed form of the Archaeoglobus fulgidus ferritin by site directed mutagenesis==
 <StructureSection load='3kx9' size='340' side='right' caption='[[3kx9]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1s3q|1s3q]], [[1sq3|1sq3]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AF0834, AF_0834 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2234 ARCFL])</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=3kx9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kx9 OCA], [http://pdbe.org/3kx9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3kx9 RCSB], [http://www.ebi.ac.uk/pdbsum/3kx9 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=3kx9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kx9 OCA], [http://pdbe.org/3kx9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3kx9 RCSB], [http://www.ebi.ac.uk/pdbsum/3kx9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3kx9 ProSAT]</span></td></tr>
 </table>
 <div style="background-color:#fffaf0;">

3kx9

From Proteopedia

Revision as of 07:09, 2 January 2019

Engineering a closed form of the Archaeoglobus fulgidus ferritin by site directed mutagenesis

Structural highlights

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox