5enl

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="5enl" size="450" color="white" frame="true" align="right" spinBox="true" caption="5enl, resolution 2.2&Aring;" /> '''INHIBITION OF ENOLASE...)
Current revision (14:08, 13 March 2024) (edit) (undo)
 
(13 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:5enl.gif|left|200px]]<br /><applet load="5enl" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="5enl, resolution 2.2&Aring;" />
 
-
'''INHIBITION OF ENOLASE: THE CRYSTAL STRUCTURES OF ENOLASE-CA2+-PHOSPHOGLYCERATE AND ENOLASE-ZN2+-PHOSPHOGLYCOLATE COMPLEXES AT 2.2-ANGSTROMS RESOLUTION'''<br />
 
-
==Overview==
+
==INHIBITION OF ENOLASE: THE CRYSTAL STRUCTURES OF ENOLASE-CA2+-PHOSPHOGLYCERATE AND ENOLASE-ZN2+-PHOSPHOGLYCOLATE COMPLEXES AT 2.2-ANGSTROMS RESOLUTION==
-
Enolase is a metalloenzyme which catalyzes the elimination of H2O from, 2-phosphoglyceric acid (PGA) to form phosphoenolpyruvate (PEP). Mg2+ and, Zn2+ are cofactors which strongly bind and activate the enzyme. Ca2+ also, binds strongly but does not produce activity. Phosphoglycolate (PG) is a, competitive inhibitor of enolase. The structures of two inhibitory ternary, complexes: yeast enolase-Ca2(+)-PGA and yeast enolase-Zn2(+)-PG, were, determined by X-ray diffraction to 2.2-A resolution and were refined by, crystallographic least-squares to R = 14.8% and 15.7%, respectively, with, good geometries of the models. These structures are compared with the, structure of the precatalytic ternary complex enolase-Mg2(+)-PGA/PEP, (Lebioda &amp; Stec, 1991). In the complex enolase-Ca2(+)-PGA, the PGA, molecule coordinates to the Ca2+ ion with the hydroxyl group, as in the, precatalytic complex. The conformation of the PGA molecule is however, different. In the active complex, the organic part of the PGA molecule is, planar, similar to the product. In the inhibitory complex, the carboxylic, group is in an orthonormal conformation. In the inhibitory complex, enolase-Zn2(+)-PG, the PG molecule coordinates with the carboxylic group, in a monodentate mode. In both inhibitory complexes, the conformational, changes in flexible loops, which were observed in the precatalytic, complex, do not take place. The lack of catalytic metal ion binding, suggests that these conformational changes are necessary for the formation, of the catalytic metal ion binding site.
+
<StructureSection load='5enl' size='340' side='right'caption='[[5enl]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[5enl]] is a 1 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=5ENL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ENL 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]] 2.2&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2PG:2-PHOSPHOGLYCERIC+ACID'>2PG</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</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=5enl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5enl OCA], [https://pdbe.org/5enl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5enl RCSB], [https://www.ebi.ac.uk/pdbsum/5enl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5enl ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/ENO1_YEAST ENO1_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/en/5enl_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=5enl ConSurf].
 +
<div style="clear:both"></div>
-
==About this Structure==
+
==See Also==
-
5ENL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with CA and 2PG as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phosphopyruvate_hydratase Phosphopyruvate hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.11 4.2.1.11] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=5ENL OCA].
+
*[[Enolase 3D structures|Enolase 3D structures]]
-
 
+
__TOC__
-
==Reference==
+
</StructureSection>
-
Inhibition of enolase: the crystal structures of enolase-Ca2(+)- 2-phosphoglycerate and enolase-Zn2(+)-phosphoglycolate complexes at 2.2-A resolution., Lebioda L, Stec B, Brewer JM, Tykarska E, Biochemistry. 1991 Mar 19;30(11):2823-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2007121 2007121]
+
[[Category: Large Structures]]
-
[[Category: Phosphopyruvate hydratase]]
+
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
-
[[Category: Single protein]]
+
[[Category: Lebioda L]]
-
[[Category: Lebioda, L.]]
+
[[Category: Stec B]]
-
[[Category: Stec, B.]]
+
-
[[Category: 2PG]]
+
-
[[Category: CA]]
+
-
[[Category: carbon-oxygen lyase]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:29:55 2007''
+

Current revision

INHIBITION OF ENOLASE: THE CRYSTAL STRUCTURES OF ENOLASE-CA2+-PHOSPHOGLYCERATE AND ENOLASE-ZN2+-PHOSPHOGLYCOLATE COMPLEXES AT 2.2-ANGSTROMS RESOLUTION

PDB ID 5enl

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/5enl"
Personal tools