View source for 4aaj


==Structure of N-(5'-phosphoribosyl)anthranilate isomerase from Pyrococcus furiosus==
<StructureSection load='4aaj' size='340' side='right'caption='[[4aaj]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4aaj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AAJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AAJ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4aaj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4aaj OCA], [https://pdbe.org/4aaj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4aaj RCSB], [https://www.ebi.ac.uk/pdbsum/4aaj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4aaj ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TRPF_PYRFU TRPF_PYRFU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The structure of phosphoribosyl anthranilate isomerase (TrpF) from the hyperthermophilic archaeon Pyrococcus furiosus (PfTrpF) has been determined at 1.75 A resolution. The PfTrpF structure has a monomeric TIM-barrel fold which differs from the dimeric structures of two other known thermophilic TrpF proteins. A comparison of the PfTrpF structure with the two known bacterial thermophilic TrpF structures and the structure of a related mesophilic protein from Escherichia coli (EcTrpF) is presented. The thermophilic TrpF structures contain a higher proportion of ion pairs and charged residues compared with the mesophilic EcTrpF. These residues contribute to the closure of the central barrel and the stabilization of the barrel and the surrounding alpha-helices. In the monomeric PfTrpF conserved structural water molecules are mostly absent; instead, the structural waters are replaced by direct side-chain-main-chain interactions. As a consequence of these combined mechanisms, the P. furiosus enzyme is a thermodynamically stable and entropically optimized monomeric TIM-barrel enzyme which defines a good framework for further protein engineering for industrial applications.

A monomeric TIM-barrel structure from Pyrococcus furiosus is optimized for extreme temperatures.,Repo H, Oeemig JS, Djupsjobacka J, Iwai H, Heikinheimo P Acta Crystallogr D Biol Crystallogr. 2012 Nov;68(Pt 11):1479-87. doi:, 10.1107/S0907444912037171. Epub 2012 Oct 13. PMID:23090397<ref>PMID:23090397</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4aaj" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pyrococcus furiosus]]
[[Category: Djupsjobacka JB]]
[[Category: Heikinheimo P]]
[[Category: Iwai H]]
[[Category: Oeemig JS]]
[[Category: Repo H]]