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[[Image:1eps.jpg|left|200px]]<br /><applet load="1eps" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1eps, resolution 3.0&Aring;" />
'''STRUCTURE AND TOPOLOGICAL SYMMETRY OF THE GLYPHOSPHATE 5-ENOL-PYRUVYLSHIKIMATE-3-PHOSPHATE SYNTHASE: A DISTINCTIVE PROTEIN FOLD'''<br />


==Overview==
==STRUCTURE AND TOPOLOGICAL SYMMETRY OF THE GLYPHOSPHATE 5-ENOL-PYRUVYLSHIKIMATE-3-PHOSPHATE SYNTHASE: A DISTINCTIVE PROTEIN FOLD==
5-enol-Pyruvylshikimate-3-phosphate synthase (EPSP synthase; phosphoenolpyruvate:3-phosphoshikimate 1-carboxyvinyltransferase, EC 2.5.1.19) is an enzyme on the pathway toward the synthesis of aromatic amino acids in plants, fungi, and bacteria and is the target of the broad-spectrum herbicide glyphosate. The three-dimensional structure of the enzyme from Escherichia coli has been determined by crystallographic techniques. The polypeptide backbone chain was traced by examination of an electron density map calculated at 3-A resolution. The two-domain structure has a distinctive fold and appears to be formed by 6-fold replication of a protein folding unit comprising two parallel helices and a four-stranded sheet. Each domain is formed from three of these units, which are related by an approximate threefold symmetry axis; in each domain three of the helices are completely buried by a surface formed from the three beta-sheets and solvent-accessible faces of the other three helices. The domains are related by an approximate dyad, but in the present crystals the molecule does not display pseudo-symmetry related to the symmetry of point group 32 because its approximate threefold axes are almost normal. A possible relation between the three-dimensional structure of the protein and the linear sequence of its gene will be described. The topological threefold symmetry and orientation of each of the two observed globular domains may direct the binding of substrates and inhibitors by a helix macrodipole effect and implies that the active site is located near the interdomain crossover segments. The structure also suggests a rationale for the glyphosate tolerance conferred by sequence alterations.
<StructureSection load='1eps' size='340' side='right'caption='[[1eps]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1eps]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EPS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EPS 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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1eps FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eps OCA], [https://pdbe.org/1eps PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eps RCSB], [https://www.ebi.ac.uk/pdbsum/1eps PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eps ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AROA_ECOLI AROA_ECOLI]
== 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/ep/1eps_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=1eps ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1EPS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Riboflavin_synthase Riboflavin synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.9 2.5.1.9] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EPS OCA].
*[[EPSP synthase 3D structures|EPSP synthase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Structure and topological symmetry of the glyphosate target 5-enolpyruvylshikimate-3-phosphate synthase: a distinctive protein fold., Stallings WC, Abdel-Meguid SS, Lim LW, Shieh HS, Dayringer HE, Leimgruber NK, Stegeman RA, Anderson KS, Sikorski JA, Padgette SR, Kishore GM, Proc Natl Acad Sci U S A. 1991 Jun 1;88(11):5046-50. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11607190 11607190]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Riboflavin synthase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Abdel-Meguid SS]]
[[Category: Abdel-Meguid, S S.]]
[[Category: Anderson KS]]
[[Category: Anderson, K S.]]
[[Category: Dayringer HE]]
[[Category: Dayringer, H E.]]
[[Category: Kishore GM]]
[[Category: Kishore, G M.]]
[[Category: Leimgruber NK]]
[[Category: Leimgruber, N K.]]
[[Category: Lim LW]]
[[Category: Lim, L W.]]
[[Category: Padgette SR]]
[[Category: Padgette, S R.]]
[[Category: Shieh H-S]]
[[Category: Shieh, H S.]]
[[Category: Sikorski JA]]
[[Category: Sikorski, J A.]]
[[Category: Stallings WC]]
[[Category: Stallings, W C.]]
[[Category: Stegeman RA]]
[[Category: Stegeman, R A.]]
[[Category: transferase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:30:24 2008''

Latest revision as of 07:05, 7 February 2024

STRUCTURE AND TOPOLOGICAL SYMMETRY OF THE GLYPHOSPHATE 5-ENOL-PYRUVYLSHIKIMATE-3-PHOSPHATE SYNTHASE: A DISTINCTIVE PROTEIN FOLD

1eps, resolution 3.00Å

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