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[[Image:1e4o.jpg|left|200px]]


{{Structure
==Phosphorylase recognition and phosphorolysis of its oligosaccharide substrate: answers to a long outstanding question==
|PDB= 1e4o |SIZE=350|CAPTION= <scene name='initialview01'>1e4o</scene>, resolution 2.9&Aring;
<StructureSection load='1e4o' size='340' side='right'caption='[[1e4o]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
|SITE= <scene name='pdbsite=PLA:Plp+Binding+Site+For+Chain+A+The+Catalytic+Site+Has+The+...'>PLA</scene> and <scene name='pdbsite=PLB:Plp+Binding+Site+For+Chain+B'>PLB</scene>
== Structural highlights ==
|LIGAND= <scene name='pdbligand=GLC:GLUCOSE'>GLC</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5&#39;-PHOSPHATE'>PLP</scene>
<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>
|ACTIVITY= <span class='plainlinks'>[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] </span>
</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>
|GENE=
<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>
|DOMAIN=
<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>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e4o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e4o OCA], [http://www.ebi.ac.uk/pdbsum/1e4o PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1e4o RCSB]</span>
== 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 ==
'''PHOSPHORYLASE RECOGNITION AND PHOSPHOROLYSIS OF ITS OLIGOSACCHARIDE SUBSTRATE: ANSWERS TO A LONG OUTSTANDING QUESTION'''
[[Image:Consurf_key_small.gif|200px|right]]
 
Check<jmol>
 
  <jmolCheckbox>
==Overview==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e4/1e4o_consurf.spt"</scriptWhenChecked>
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.
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 
    <text>to colour the structure by Evolutionary Conservation</text>
==About this Structure==
  </jmolCheckbox>
1E4O is a [[Single protein]] structure of sequence from [http://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].  
</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>
==Reference==
__TOC__
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://www.ncbi.nlm.nih.gov/pubmed/10469642 10469642]
</StructureSection>
[[Category: Escherichia coli]]
[[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: binary and ternary oligosaccharide complex]]
[[Category: carbohydrate recognition]]
[[Category: maltopentaose]]
[[Category: phosphorylase mechanism]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:55:05 2008''

Latest revision as of 12:58, 20 March 2024

Phosphorylase recognition and phosphorolysis of its oligosaccharide substrate: answers to a long outstanding questionPhosphorylase recognition and phosphorolysis of its oligosaccharide substrate: answers to a long outstanding question

Structural highlights

1e4o is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.9Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

1e4o, resolution 2.90Å

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OCA
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