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[[Image:1hfb.gif|left|200px]]


{{Structure
==Crystal structure of the tyrosine-regulated 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Saccharomyces cerevisiae complexed with phosphoenolpyruvate==
|PDB= 1hfb |SIZE=350|CAPTION= <scene name='initialview01'>1hfb</scene>, resolution 1.9&Aring;
<StructureSection load='1hfb' size='340' side='right'caption='[[1hfb]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
|SITE= <scene name='pdbsite=AC1:Pep+Binding+Site+For+Chain+H'>AC1</scene>
== Structural highlights ==
|LIGAND= <scene name='pdbligand=PEP:PHOSPHOENOLPYRUVATE'>PEP</scene>
<table><tr><td colspan='2'>[[1hfb]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HFB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HFB FirstGlance]. <br>
|ACTIVITY= [http://en.wikipedia.org/wiki/Transferred_entry:_2.5.1.54 Transferred entry: 2.5.1.54], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.15 4.1.2.15]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEP:PHOSPHOENOLPYRUVATE'>PEP</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=1hfb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hfb OCA], [https://pdbe.org/1hfb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hfb RCSB], [https://www.ebi.ac.uk/pdbsum/1hfb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hfb ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AROG_YEAST AROG_YEAST] Stereospecific condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP).
== 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/hf/1hfb_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1hfb ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The betaalpha barrel is the common protein fold of numerous enzymes and was proposed recently to be the result of gene duplication and fusion of an ancient half-barrel. The initial enzyme of shikimate biosynthesis possesses the additional feature of feedback regulation. The crystal structure and kinetic studies on chimera and mutant proteins of yeast 3-deoxy-d-arabino-heptulosonate-7-phosphate (DAHP) synthase from Saccharomyces cerevisiae inhibited by phenylalanine (Aro3p) and DAHP synthase S. cerevisiae inhibited by tyrosine (Aro4p) give insight into important regions for regulation in the enzyme: The loop, which is connecting the two half-barrels, and structural elements added to the barrel are prerequisites for regulation and form a cavity on the N-terminal side of the betaalpha barrel. In the cavity of Aro4p at position 226 is a glycine residue, which is highly conserved in all other tyrosine-regulated DAHP synthases as well. Sequence alignments with phenylalanine-regulated DAHP synthases including Aro3p show a highly conserved serine residue at this position. An exchange of glycine to serine and vice versa leads to a complete change in the regulation pattern. Therefore the evolution of these differently feedback-inhibited isoenzymes required gene duplication and a single mutation within the internal extra element. Numerous additional amino acid substitutions present in the contemporary isoenzymes are irrelevant for regulation and occurred independently.


'''CRYSTAL STRUCTURE OF THE TYROSINE-REGULATED 3-DEOXY-D-ARABINO-HEPTULOSONATE-7-PHOSPHATE SYNTHASE FROM SACCHAROMYCES CEREVISIAE COMPLEXED WITH PHOSPHOENOLPYRUVATE'''
Evolution of feedback-inhibited beta /alpha barrel isoenzymes by gene duplication and a single mutation.,Hartmann M, Schneider TR, Pfeil A, Heinrich G, Lipscomb WN, Braus GH Proc Natl Acad Sci U S A. 2003 Feb 4;100(3):862-7. Epub 2003 Jan 22. PMID:12540830<ref>PMID:12540830</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1hfb" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
The betaalpha barrel is the common protein fold of numerous enzymes and was proposed recently to be the result of gene duplication and fusion of an ancient half-barrel. The initial enzyme of shikimate biosynthesis possesses the additional feature of feedback regulation. The crystal structure and kinetic studies on chimera and mutant proteins of yeast 3-deoxy-d-arabino-heptulosonate-7-phosphate (DAHP) synthase from Saccharomyces cerevisiae inhibited by phenylalanine (Aro3p) and DAHP synthase S. cerevisiae inhibited by tyrosine (Aro4p) give insight into important regions for regulation in the enzyme: The loop, which is connecting the two half-barrels, and structural elements added to the barrel are prerequisites for regulation and form a cavity on the N-terminal side of the betaalpha barrel. In the cavity of Aro4p at position 226 is a glycine residue, which is highly conserved in all other tyrosine-regulated DAHP synthases as well. Sequence alignments with phenylalanine-regulated DAHP synthases including Aro3p show a highly conserved serine residue at this position. An exchange of glycine to serine and vice versa leads to a complete change in the regulation pattern. Therefore the evolution of these differently feedback-inhibited isoenzymes required gene duplication and a single mutation within the internal extra element. Numerous additional amino acid substitutions present in the contemporary isoenzymes are irrelevant for regulation and occurred independently.
*[[DAHP synthase 3D structures|DAHP synthase 3D structures]]
 
== References ==
==About this Structure==
<references/>
1HFB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HFB OCA].
__TOC__
 
</StructureSection>
==Reference==
[[Category: Large Structures]]
Evolution of feedback-inhibited beta /alpha barrel isoenzymes by gene duplication and a single mutation., Hartmann M, Schneider TR, Pfeil A, Heinrich G, Lipscomb WN, Braus GH, Proc Natl Acad Sci U S A. 2003 Feb 4;100(3):862-7. Epub 2003 Jan 22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12540830 12540830]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Braus GH]]
[[Category: Transferred entry: 2 5.1 54]]
[[Category: Hartmann M]]
[[Category: Braus, G H.]]
[[Category: Schneider TR]]
[[Category: Hartmann, M.]]
[[Category: Schneider, T R.]]
[[Category: PEP]]
[[Category: beta-alpha-barrel]]
[[Category: lyase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:36:23 2008''
Retrieved from "https://proteopedia.org/1hfb"