We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2hls

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (05:15, 17 October 2024) (edit) (undo)
 
(11 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:2hls.png|left|200px]]
 
-
<!--
+
==The crystal structure of a protein disulfide oxidoreductase from Aeropyrum pernix k1==
-
The line below this paragraph, containing "STRUCTURE_2hls", creates the "Structure Box" on the page.
+
<StructureSection load='2hls' size='340' side='right'caption='[[2hls]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[2hls]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aeropyrum_pernix_K1 Aeropyrum pernix K1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HLS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HLS FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.93&#8491;</td></tr>
-
-->
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
-
{{STRUCTURE_2hls| PDB=2hls | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2hls FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hls OCA], [https://pdbe.org/2hls PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hls RCSB], [https://www.ebi.ac.uk/pdbsum/2hls PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hls ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/Q9YDZ4_AERPE Q9YDZ4_AERPE]
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hl/2hls_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2hls ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The formation of disulfide bonds between cysteine residues is a rate-limiting step in protein folding. To control this oxidative process, different organisms have developed different systems. In bacteria, disulfide bond formation is assisted by the Dsb protein family; in eukarya, disulfide bond formation and rearrangement are catalyzed by PDI. In thermophilic organisms, a potential key role in disulfide bond formation has recently been ascribed to a new cytosolic Protein Disulphide Oxidoreductase family whose members have a molecular mass of about 26 kDa and are characterized by two thioredoxin folds comprising a CXXC active site motif each. Here we report on the functional and structural characterization of ApPDO, a new member of this family, which was isolated from the archaeon Aeropyrum pernix K1. Functional studies have revealed that ApPDO can catalyze the reduction, oxidation and isomerization of disulfide bridges. Structural studies have shown that this protein has two CXXC active sites with fairly similar geometrical parameters typical of a stable conformation. Finally, a theoretical calculation of the cysteine pK(a) values has suggested that the two active sites have similar functional properties and each of them can impart activity to the enzyme. Our results are evidence of functional similarity between the members of the Protein Disulphide Oxidoreductase family and the eukaryotic enzyme PDI. However, as the different three-dimensional features of these two biological systems strongly suggest significantly different mechanisms of action, further experimental studies will be needed to make clear how different three-dimensional structures can result in systems with similar functional behavior.
-
===The crystal structure of a protein disulfide oxidoreductase from Aeropyrum pernix k1===
+
A novel member of the protein disulfide oxidoreductase family from Aeropyrum pernix K1: structure, function and electrostatics.,D'Ambrosio K, Pedone E, Langella E, De Simone G, Rossi M, Pedone C, Bartolucci S J Mol Biol. 2006 Sep 29;362(4):743-52. Epub 2006 Jul 28. PMID:16934838<ref>PMID:16934838</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 2hls" style="background-color:#fffaf0;"></div>
-
<!--
+
==See Also==
-
The line below this paragraph, {{ABSTRACT_PUBMED_16934838}}, adds the Publication Abstract to the page
+
*[[Protein disulfide oxidoreductase 3D structures|Protein disulfide oxidoreductase 3D structures]]
-
(as it appears on PubMed at http://www.pubmed.gov), where 16934838 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_16934838}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
[[Category: Aeropyrum pernix K1]]
-
2HLS is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Aeropyrum_pernix Aeropyrum pernix]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HLS OCA].
+
[[Category: Large Structures]]
-
 
+
[[Category: D'Ambrosio K]]
-
==Reference==
+
[[Category: De Simone G]]
-
<ref group="xtra">PMID:16934838</ref><references group="xtra"/>
+
-
[[Category: Aeropyrum pernix]]
+
-
[[Category: Ambrosio, K D.]]
+
-
[[Category: Simone, G De.]]
+
-
[[Category: Protein disulfide oxidoreductase]]
+
-
[[Category: Thioredoxin fold]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 08:56:33 2009''
+

Current revision

The crystal structure of a protein disulfide oxidoreductase from Aeropyrum pernix k1

PDB ID 2hls

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/2hls"
Personal tools