1ahp

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[[Image:1ahp.gif|left|200px]]
 
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{{Structure
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==OLIGOSACCHARIDE SUBSTRATE BINDING IN ESCHERICHIA COLI MALTODEXTRIN PHSPHORYLASE==
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|PDB= 1ahp |SIZE=350|CAPTION= <scene name='initialview01'>1ahp</scene>, resolution 3.0&Aring;
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<StructureSection load='1ahp' size='340' side='right'caption='[[1ahp]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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|SITE= <scene name='pdbsite=1:Catalytic+Site+Is+Located+At+The+Base+Of+A+Cleft+Between+...'>1</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAL:MALTOSE'>MAL</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5&#39;-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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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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|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>
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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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|GENE=
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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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|DOMAIN=
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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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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ahp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ahp OCA], [http://www.ebi.ac.uk/pdbsum/1ahp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ahp RCSB]</span>
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== Function ==
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}}
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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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'''OLIGOSACCHARIDE SUBSTRATE BINDING IN ESCHERICHIA COLI MALTODEXTRIN PHSPHORYLASE'''
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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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==Overview==
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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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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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<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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==About this Structure==
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</jmolCheckbox>
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1AHP 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=1AHP OCA].
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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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==Reference==
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__TOC__
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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://www.ncbi.nlm.nih.gov/pubmed/9145112 9145112]
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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: 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 Sun Mar 30 18:40:25 2008''
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Current revision

OLIGOSACCHARIDE SUBSTRATE BINDING IN ESCHERICHIA COLI MALTODEXTRIN PHSPHORYLASE

PDB ID 1ahp

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