1e4o: Difference between revisions

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-[[Image:1e4o.gif|left|200px]]<br />
-<applet load="1e4o" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1e4o, resolution 2.9&Aring;" />
-'''PHOSPHORYLASE RECOGNITION AND PHOSPHOROLYSIS OF ITS OLIGOSACCHARIDE SUBSTRATE: ANSWERS TO A LONG OUTSTANDING QUESTION'''<br />
-==Overview==
+==Phosphorylase recognition and phosphorolysis of its oligosaccharide substrate: answers to a long outstanding question==
-Phosphorylases are key enzymes of carbohydrate metabolism. Structural, studies have provided explanations for almost all features of control and, substrate recognition of phosphorylase but one question remains, unanswered. How does phosphorylase recognize and cleave an oligosaccharide, substrate? To answer this question we turned to the Escherichia coli, maltodextrin phosphorylase (MalP), a non-regulatory phosphorylase that, shares similar kinetic and catalytic properties with the mammalian, glycogen phosphorylase. The crystal structures of three, MalP-oligosaccharide complexes are reported: the binary complex of MalP, with the natural substrate, maltopentaose (G5); the binary complex with, the thio-oligosaccharide, 4-S-alpha-D-glucopyranosyl-4-thiomaltotetraose, (GSG4), both at 2.9 A resolution; and the 2.1 A resolution ternary complex, of MalP with thio-oligosaccharide and phosphate (GSG4-P). The results show, a pentasaccharide bound across the catalytic site of MalP with sugars, occupying sub-sites -1 to +4. Binding of GSG4 is identical to the natural, pentasaccharide, indicating that the inactive thio compound is a close, mimic of the natural substrate. The ternary MalP-GSG4-P complex shows the, phosphate group poised to attack the glycosidic bond and promote, phosphorolysis. In all three complexes the pentasaccharide exhibits an, altered conformation across sub-sites -1 and +1, the site of catalysis, from the preferred conformation for alpha(1-4)-linked glucosyl polymers.
+<StructureSection load='1e4o' size='340' side='right'caption='[[1e4o]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
+== Structural highlights ==
-==About this Structure==
+<table><tr><td colspan='2'>[[1e4o]] is a 2 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=1E4O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E4O FirstGlance]. <br>
-E4O is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with PLP as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Phosphorylase Phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.1 2.4.1.1] Structure known Active Sites: PLA and PLB. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E4O OCA].
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
-==Reference==
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1e4o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e4o OCA], [https://pdbe.org/1e4o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e4o RCSB], [https://www.ebi.ac.uk/pdbsum/1e4o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e4o ProSAT]</span></td></tr>
-Phosphorylase recognition and phosphorolysis of its oligosaccharide substrate: answers to a long outstanding question., Watson KA, McCleverty C, Geremia S, Cottaz S, Driguez H, Johnson LN, EMBO J. 1999 Sep 1;18(17):4619-32. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10469642 10469642]
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/PHSM_ECOLI PHSM_ECOLI] Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.
+== 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/e4/1e4o_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=1e4o ConSurf].
+<div style="clear:both"></div>
+__TOC__
+</StructureSection>
 [[Category: Escherichia coli]]
-[[Category: Phosphorylase]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Cottaz S]]
-[[Category: Cottaz, S.]]
+[[Category: Driguez H]]
-[[Category: Driguez, H.]]
+[[Category: Geremia S]]
-[[Category: Geremia, S.]]
+[[Category: Johnson LN]]
-[[Category: Johnson, L.N.]]
+[[Category: McCleverty C]]
-[[Category: Mccleverty, C.]]
+[[Category: Watson KA]]
-[[Category: Watson, K.A.]]
-[[Category: PLP]]
-[[Category: binary and ternary oligosaccharide complexes]]
-[[Category: carbohydrate recognition]]
-[[Category: maltopentaose]]
-[[Category: phosphorylase mechanism]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov  5 12:23:18 2007''