This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1r52

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (13:29, 13 March 2024) (edit) (undo)
 
(13 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1r52.jpg|left|200px]]<br /><applet load="1r52" size="350" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1r52, resolution 2.89&Aring;" />
 
-
'''Crystal structure of the bifunctional chorismate synthase from Saccharomyces cerevisiae'''<br />
 
-
==Overview==
+
==Crystal structure of the bifunctional chorismate synthase from Saccharomyces cerevisiae==
-
Chorismate synthase (EC 4.2.3.5), the seventh enzyme in the shikimate pathway, catalyzes the transformation of 5-enolpyruvylshikimate 3-phosphate (EPSP) to chorismate, which is the last common precursor in the biosynthesis of numerous aromatic compounds in bacteria, fungi, and plants. The chorismate synthase reaction involves a 1,4-trans-elimination of phosphoric acid from EPSP and has an absolute requirement for reduced FMN as a cofactor. We have determined the three-dimensional x-ray structure of the yeast chorismate synthase from selenomethionine-labeled crystals at 2.2-A resolution. The structure shows a novel betaalphabetaalpha fold consisting of an alternate tight packing of two alpha-helical and two beta-sheet layers, showing no resemblance to any documented protein structure. The molecule is arranged as a tight tetramer with D2 symmetry, in accordance with its quaternary structure in solution. Electron density is missing for 23% of the amino acids, spread over sequence regions that in the three-dimensional structure converge on the surface of the protein. Many totally conserved residues are contained within these regions, and they probably form a structured but mobile domain that closes over a cleft upon substrate binding and catalysis. This hypothesis is supported by previously published spectroscopic measurements implying that the enzyme undergoes considerable structural changes upon binding of both FMN and EPSP.
+
<StructureSection load='1r52' size='340' side='right'caption='[[1r52]], [[Resolution|resolution]] 2.89&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1r52]] is a 4 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=1R52 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R52 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]] 2.89&#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=1r52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r52 OCA], [https://pdbe.org/1r52 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r52 RCSB], [https://www.ebi.ac.uk/pdbsum/1r52 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r52 ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/AROC_YEAST AROC_YEAST]
 +
== 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/r5/1r52_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=1r52 ConSurf].
 +
<div style="clear:both"></div>
-
==About this Structure==
+
==See Also==
-
1R52 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Active as [http://en.wikipedia.org/wiki/Chorismate_synthase Chorismate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.3.5 4.2.3.5] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R52 OCA].
+
*[[Chorismate synthase|Chorismate synthase]]
-
 
+
__TOC__
-
==Reference==
+
</StructureSection>
-
Crystal structure of the bifunctional chorismate synthase from Saccharomyces cerevisiae., Quevillon-Cheruel S, Leulliot N, Meyer P, Graille M, Bremang M, Blondeau K, Sorel I, Poupon A, Janin J, van Tilbeurgh H, J Biol Chem. 2004 Jan 2;279(1):619-25. Epub 2003 Oct 21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14573601 14573601]
+
[[Category: Large Structures]]
-
[[Category: Chorismate synthase]]
+
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
-
[[Category: Single protein]]
+
[[Category: Blondeau K]]
-
[[Category: Blondeau, K.]]
+
[[Category: Bremang M]]
-
[[Category: Bremang, M.]]
+
[[Category: Graille M]]
-
[[Category: Graille, M.]]
+
[[Category: Janin J]]
-
[[Category: Janin, J.]]
+
[[Category: Leulliot N]]
-
[[Category: Leulliot, N.]]
+
[[Category: Meyer P]]
-
[[Category: Meyer, P.]]
+
[[Category: Poupon A]]
-
[[Category: Poupon, A.]]
+
[[Category: Quevillon-Cheruel S]]
-
[[Category: Quevillon-Cheruel, S.]]
+
[[Category: Sorel I]]
-
[[Category: Sorel, I.]]
+
[[Category: Van Tilbeurgh H]]
-
[[Category: Tilbeurgh, H van.]]
+
-
[[Category: two layers alpha-beta]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:47:13 2008''
+

Current revision

Crystal structure of the bifunctional chorismate synthase from Saccharomyces cerevisiae

PDB ID 1r52

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1r52"
Personal tools