1ahp

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[[Image:1ahp.gif|left|200px]]<br /><applet load="1ahp" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ahp, resolution 3.0&Aring;" />
 
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'''OLIGOSACCHARIDE SUBSTRATE BINDING IN ESCHERICHIA COLI MALTODEXTRIN PHSPHORYLASE'''<br />
 
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==Overview==
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==OLIGOSACCHARIDE SUBSTRATE BINDING IN ESCHERICHIA COLI MALTODEXTRIN PHSPHORYLASE==
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The crystal structure of E. coli maltodextrin phosphorylase co-crystallized with an oligosaccharide has been solved at 3.0 A resolution, providing the first structure of an oligosaccharide bound at the catalytic site of an alpha-glucan phosphorylase. An induced fit mechanism brings together two domains across the catalytic site tunnel. A stacking interaction between the glucosyl residue and the aromatic group of a tyrosine residue at a sub-site remote (8 A) from the catalytic site provides a key element in substrate recognition; mutation of this residue to Ala decreases the Kcat/Km by 10(4). Extrapolation of the results to substrate binding across the site of attack by phosphorolysis indicates a likely alteration in the glycosidic torsion angles from their preferred values, an alteration that appears to be important for the catalytic mechanism.
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<StructureSection load='1ahp' size='340' side='right'caption='[[1ahp]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1ahp]] 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=1AHP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AHP FirstGlance]. <br>
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1AHP 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 <scene name='pdbligand=MAL:'>MAL</scene>, <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=PLP:'>PLP</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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] Known structural/functional Site: <scene name='pdbsite=1:Catalytic+Site+Is+Located+At+The+Base+Of+A+Cleft+Between+...'>1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AHP OCA].
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</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>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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==Reference==
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ahp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ahp OCA], [https://pdbe.org/1ahp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ahp RCSB], [https://www.ebi.ac.uk/pdbsum/1ahp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ahp ProSAT]</span></td></tr>
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Oligosaccharide substrate binding in Escherichia coli maltodextrin phosphorylase., O'Reilly M, Watson KA, Schinzel R, Palm D, Johnson LN, Nat Struct Biol. 1997 May;4(5):405-12. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9145112 9145112]
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ah/1ahp_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1ahp ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Phosphorylase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Johnson LN]]
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[[Category: Johnson, L N.]]
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[[Category: O'Reilly M]]
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[[Category: Palm, D.]]
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[[Category: Palm D]]
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[[Category: Reilly, M O.]]
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[[Category: Schinzel R]]
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[[Category: Schinzel, R.]]
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[[Category: Watson KA]]
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[[Category: Watson, K A.]]
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[[Category: GOL]]
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[[Category: MAL]]
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[[Category: PLP]]
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[[Category: SO4]]
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[[Category: ecoli]]
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[[Category: induced-fit]]
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[[Category: maltodextrin]]
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[[Category: oligosaccharide]]
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[[Category: phosphorylase]]
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[[Category: stacking]]
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[[Category: substrate]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:44:35 2008''
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Current revision

OLIGOSACCHARIDE SUBSTRATE BINDING IN ESCHERICHIA COLI MALTODEXTRIN PHSPHORYLASE

PDB ID 1ahp

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