3sid

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:3sid.png|left|200px]]
+
==Crystal structure of oxidized Symerythrin from Cyanophora paradoxa, azide adduct at 50% occupancy==
 +
<StructureSection load='3sid' size='340' side='right' caption='[[3sid]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[3sid]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cyanophora_paradoxa Cyanophora paradoxa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SID OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SID FirstGlance]. <br>
 +
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AZI:AZIDE+ION'>AZI</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene><br>
 +
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3qhb|3qhb]], [[3qhc|3qhc]]</td></tr>
 +
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Cyanelle ORF180 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2762 Cyanophora paradoxa])</td></tr>
 +
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3sid FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sid OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3sid RCSB], [http://www.ebi.ac.uk/pdbsum/3sid PDBsum]</span></td></tr>
 +
<table>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Rubrerythrins are diiron-containing peroxidases that belong to the ferritin-like superfamily (FLSF). Here, we describe the structures of symerythrin, a novel rubrerythrin variant from the oxygenic phototroph Cyanophora paradoxa, at 1.20-1.40 A resolution in three different states: diferric, azide-bound diferric and chemically reduced. The symerythrin metallocenter has a unique eighth ligating residue compared to rubrerythrin-an additional glutamate inserted into helix A of the four-helix bundle that resides on a pi-helical segment. Otherwise, the diferric metallocenter structure is highly similar to that of characterized rubrerythrins. Azide binds the diferric center in a mu-1,1 orientation similar to how peroxide binds to diferric rubrerythrin. The structure of the diferrous metallocenter shows heterogeneity that we ascribe to the acidic pH of the crystals. In what we consider the neutral pH conformation, reduction causes a 2.0-A shift in Fe1 and the toggling of a Glu to a His ligand, as seen with rubrerythrins. The function of symerythrin remains unknown, but preliminary tests showing oxidase and peroxidase activities and the similarities of its metallocenter to other rubrerythrins suggest similar functionalities between the two despite the additional ligating glutamate in symerythrin. Of particular interest is the high internal symmetry of symerythrin, which supports the notion that its core four-helix bundle was formed by the gene duplication and fusion of a two-helix peptide. Sequence comparisons with another family in the FLSF that also has notable internal symmetry provide compelling evidence that, contrary to previous assumptions, there have been multiple gene fusion events that have generated the single-chain FLSF fold.
-
<!--
+
Symerythrin structures at atomic resolution and the origins of rubrerythrins and the ferritin-like superfamily.,Cooley RB, Arp DJ, Karplus PA J Mol Biol. 2011 Oct 14;413(1):177-94. Epub 2011 Aug 19. PMID:21872605<ref>PMID:21872605</ref>
-
The line below this paragraph, containing "STRUCTURE_3sid", creates the "Structure Box" on the page.
+
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
-
or leave the SCENE parameter empty for the default display.
+
-
-->
+
-
{{STRUCTURE_3sid| PDB=3sid | SCENE= }}
+
-
===Crystal structure of oxidized Symerythrin from Cyanophora paradoxa, azide adduct at 50% occupancy===
+
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-
 
+
</div>
-
 
+
== References ==
-
<!--
+
<references/>
-
The line below this paragraph, {{ABSTRACT_PUBMED_21872605}}, adds the Publication Abstract to the page
+
__TOC__
-
(as it appears on PubMed at http://www.pubmed.gov), where 21872605 is the PubMed ID number.
+
</StructureSection>
-
-->
+
-
{{ABSTRACT_PUBMED_21872605}}
+
-
 
+
-
==About this Structure==
+
-
[[3sid]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cyanophora_paradoxa Cyanophora paradoxa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SID OCA].
+
-
 
+
-
==Reference==
+
-
<ref group="xtra">PMID:021872605</ref><references group="xtra"/>
+
[[Category: Cyanophora paradoxa]]
[[Category: Cyanophora paradoxa]]
[[Category: Arp, D J.]]
[[Category: Arp, D J.]]

Revision as of 05:18, 5 June 2014

Crystal structure of oxidized Symerythrin from Cyanophora paradoxa, azide adduct at 50% occupancy

3sid, resolution 1.40Å

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/3sid"
Views
Personal tools
Navigation
Toolbox