View source for 4grs


==Crystal structure of a chimeric DAH7PS==
<StructureSection load='4grs' size='340' side='right'caption='[[4grs]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4grs]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus_DSM_3638 Pyrococcus furiosus DSM 3638] and [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GRS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GRS 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]] 3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TYR:TYROSINE'>TYR</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=4grs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4grs OCA], [https://pdbe.org/4grs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4grs RCSB], [https://www.ebi.ac.uk/pdbsum/4grs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4grs ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AROF_THEMA AROF_THEMA] Catalyzes the condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP).[https://www.uniprot.org/uniprot/Q8U0A9_PYRFU Q8U0A9_PYRFU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Allosteric regulation of protein function is a critical component of metabolic control. Its importance is underpinned by the diversity of mechanisms and its presence in all three domains of life. The first enzyme of the aromatic amino acid biosynthesis, 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase, shows remarkable variation in allosteric response and machinery, and both contemporary regulated and unregulated orthologs have been described. To examine the molecular events by which allostery can evolve, we have generated a chimeric protein by joining the catalytic domain of an unregulated 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase with the regulatory domain of a regulated enzyme. We demonstrate that this simple gene fusion event on its own is sufficient to confer functional allostery to the unregulated enzyme. The fusion protein shares structural similarities with its regulated parent protein and undergoes an analogous major conformational change in response to the binding of allosteric effector tyrosine to the regulatory domain. These findings help delineate a remarkably facile mechanism for the evolution of modular allostery by domain recruitment.

Engineering allosteric control to an unregulated enzyme by transfer of a regulatory domain.,Cross PJ, Allison TM, Dobson RC, Jameson GB, Parker EJ Proc Natl Acad Sci U S A. 2013 Jan 23. PMID:23345433<ref>PMID:23345433</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4grs" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pyrococcus furiosus DSM 3638]]
[[Category: Thermotoga maritima MSB8]]
[[Category: Allison TM]]
[[Category: Cross PJ]]
[[Category: Dobson RCJ]]
[[Category: Jameson GB]]
[[Category: Parker EJ]]