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.


3vnx

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:40, 20 March 2024) (edit) (undo)
 
(One intermediate revision not shown.)
Line 1: Line 1:
==Crystal structure of ferritin from multicellular green algae, Ulva pertusa.==
==Crystal structure of ferritin from multicellular green algae, Ulva pertusa.==
-
<StructureSection load='3vnx' size='340' side='right' caption='[[3vnx]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
+
<StructureSection load='3vnx' size='340' side='right'caption='[[3vnx]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[3vnx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Sea_lettuce Sea lettuce]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VNX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VNX FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[3vnx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ulva_pertusa Ulva pertusa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VNX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VNX FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ferroxidase Ferroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.16.3.1 1.16.3.1] </span></td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=3vnx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vnx OCA], [http://pdbe.org/3vnx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3vnx RCSB], [http://www.ebi.ac.uk/pdbsum/3vnx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3vnx ProSAT]</span></td></tr>
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3vnx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vnx OCA], [https://pdbe.org/3vnx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vnx RCSB], [https://www.ebi.ac.uk/pdbsum/3vnx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vnx ProSAT]</span></td></tr>
</table>
</table>
-
<div style="background-color:#fffaf0;">
+
== Function ==
-
== Publication Abstract from PubMed ==
+
[https://www.uniprot.org/uniprot/H7CGH2_ULVPE H7CGH2_ULVPE] Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation.[ARBA:ARBA00025111] Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation.[RuleBase:RU361145]
-
Plant ferritins have some unique structural and functional features. Most of these features can be related to the plant-specific 'extension peptide' (EP), which exists in the N-terminus of the mature region of a plant ferritin. Recent crystallographic analysis of a plant ferritin revealed the structure of the EP, however, two points remain unclear: (i) whether the structures of well-conserved EP of plant ferritins are common in all plants, and (ii) whether the EP truly contributes to the shell stability of the plant ferritin oligomer. To clarify these matters, we have cloned a green-plant-type ferritin cDNA from a green alga, Ulva pertusa, and investigated its crystal structure. Ulva pertusa ferritin (UpFER) has a plant-ferritin-specific extension peptide composed of 28 amino acid residues. In the crystal structure of UpFER, the EP lay on and interacted with the neighboring three-fold symmetry-related subunit. The amino acid residues involved in the interaction were very highly conserved among plant ferritins. The EPs masked the hydrophobic pockets on the ferritin shell surface by lying on them, and this made the ferritin oligomer more hydrophilic. Furthermore, differential scanning calorimetric analysis of the native and its EP-deletion mutant suggested that the EP contributed to the thermal stability of the plant ferritin shell. Thus, the shell stability and surface hydrophobicity of plant ferritin were controlled by the presence or absence of the plant-ferritin-specific EP. This regulation can account for those processes such as shell stability, degradation and association of plant ferritin, which are significantly related to iron utilization in plants.
+
-
 
+
-
The extension peptide of plant ferritin from sea lettuce contributes to shell stability and surface hydrophobicity.,Masuda T, Morimoto SI, Mikami B, Toyohara H Protein Sci. 2012 Mar 14. doi: 10.1002/pro.2061. PMID:22419613<ref>PMID:22419613</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 3vnx" style="background-color:#fffaf0;"></div>
+
==See Also==
==See Also==
-
*[[Ferritin|Ferritin]]
+
*[[Ferritin 3D structures|Ferritin 3D structures]]
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Ferroxidase]]
+
[[Category: Large Structures]]
-
[[Category: Sea lettuce]]
+
[[Category: Ulva pertusa]]
-
[[Category: Masuda, T]]
+
[[Category: Masuda T]]
-
[[Category: Mikami, B]]
+
[[Category: Mikami B]]
-
[[Category: Morimoto, S I]]
+
[[Category: Morimoto SI]]
-
[[Category: Toyohara, H]]
+
[[Category: Toyohara H]]
-
[[Category: 4-helix bundle]]
+
-
[[Category: Iron storage]]
+
-
[[Category: Oxidoreductase]]
+

Current revision

Crystal structure of ferritin from multicellular green algae, Ulva pertusa.

PDB ID 3vnx

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3vnx"
Personal tools