View source for 5c5y


==Crystal structure of deoxyribose-phosphate aldolase from Colwellia psychrerythraea (hexagonal form)==
<StructureSection load='5c5y' size='340' side='right'caption='[[5c5y]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5c5y]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Colwellia_psychrerythraea_34H Colwellia psychrerythraea 34H]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C5Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5C5Y FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=UNL:UNKNOWN+LIGAND'>UNL</scene></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=5c5y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c5y OCA], [https://pdbe.org/5c5y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5c5y RCSB], [https://www.ebi.ac.uk/pdbsum/5c5y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5c5y ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q483R4_COLP3 Q483R4_COLP3] 
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== Publication Abstract from PubMed ==
Understanding enzyme stability and activity in extremophilic organisms is of great biotechnological interest, but many questions are still unsolved. Using 2-deoxy-D-ribose-5-phosphate aldolase (DERA) as model enzyme, we have evaluated structural and functional characteristics of different orthologs from psychrophilic, mesophilic and hyperthermophilic organisms. We present the first crystal structures of psychrophilic DERAs, revealing a dimeric organization resembling their mesophilic but not their thermophilic counterparts. Conversion into monomeric proteins showed that the native dimer interface contributes to stability only in the hyperthermophilic enzymes. Nevertheless, introduction of a disulfide bridge in the interface of a psychrophilic DERA did confer increased thermostability, suggesting a strategy for rational design of more durable enzyme variants. Constraint network analysis revealed particularly sparse interactions between the substrate pocket and its surrounding alpha-helices in psychrophilic DERAs, which indicates that a more flexible active center underlies their high turnover numbers.

Trading off stability against activity in extremophilic aldolases.,Dick M, Weiergraber OH, Classen T, Bisterfeld C, Bramski J, Gohlke H, Pietruszka J Sci Rep. 2016 Jan 19;6:17908. doi: 10.1038/srep17908. PMID:26783049<ref>PMID:26783049</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5c5y" style="background-color:#fffaf0;"></div>

==See Also==
*[[Aldolase 3D structures|Aldolase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Colwellia psychrerythraea 34H]]
[[Category: Large Structures]]
[[Category: Dick M]]
[[Category: Pietruszka J]]
[[Category: Weiergraeber OH]]