1ahp: Difference between revisions

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-[[Image:1ahp.gif|left|200px]]
- {{Structure
+==OLIGOSACCHARIDE SUBSTRATE BINDING IN ESCHERICHIA COLI MALTODEXTRIN PHSPHORYLASE==
-|PDB= 1ahp |SIZE=350|CAPTION= <scene name='initialview01'>1ahp</scene>, resolution 3.0&Aring;
+<StructureSection load='1ahp' size='340' side='right'caption='[[1ahp]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
-|SITE= <scene name='pdbsite=1:Catalytic+Site+Is+Located+At+The+Base+Of+A+Cleft+Between+...'>1</scene>
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=MAL:MALTOSE'>MAL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5&#39;-PHOSPHATE'>PLP</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
+<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>
-|ACTIVITY= [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]
+</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>
-|GENE=
+<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>
-}}
+<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>
+</table>
-'''OLIGOSACCHARIDE SUBSTRATE BINDING IN ESCHERICHIA COLI MALTODEXTRIN PHSPHORYLASE'''
+== 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 ==
-==Overview==
+[[Image:Consurf_key_small.gif|200px|right]]
-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.
+Check<jmol>
+  <jmolCheckbox>
-==About this Structure==
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ah/1ahp_consurf.spt"</scriptWhenChecked>
-AHP 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].
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
-==Reference==
+  </jmolCheckbox>
-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]
+</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].
+<div style="clear:both"></div>
+__TOC__
+</StructureSection>
 [[Category: Escherichia coli]]
-[[Category: Phosphorylase]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Johnson LN]]
-[[Category: Johnson, L N.]]
+[[Category: O'Reilly M]]
-[[Category: Palm, D.]]
+[[Category: Palm D]]
-[[Category: Reilly, M O.]]
+[[Category: Schinzel R]]
-[[Category: Schinzel, R.]]
+[[Category: Watson KA]]
-[[Category: Watson, K A.]]
-[[Category: GOL]]
-[[Category: MAL]]
-[[Category: PLP]]
-[[Category: SO4]]
-[[Category: ecoli]]
-[[Category: induced-fit]]
-[[Category: maltodextrin]]
-[[Category: oligosaccharide]]
-[[Category: phosphorylase]]
-[[Category: stacking]]
-[[Category: substrate]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 11:07:11 2008''