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1ose

From Proteopedia

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[[Image:1ose.gif|left|200px]]<br />
 
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<applet load="1ose" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ose, resolution 2.30&Aring;" />
 
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'''PORCINE PANCREATIC ALPHA-AMYLASE COMPLEXED WITH ACARBOSE'''<br />
 
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==Overview==
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==Porcine pancreatic alpha-amylase complexed with acarbose==
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Two different crystal forms of pig pancreatic alpha-amylase isoenzyme II, (PPAII), free and complexed to a carbohydrate inhibitor (acarbose), have, been compared together and to previously reported structures of PPAI. A, crystal form obtained at 4 degrees C, containing nearly 72% solvent, made, it possible to obtain a new complex with acarbose, different from a, previous one obtained at 20 degrees C [Qian, M., Buisson, G., Duee, E., Haser, H. &amp; Payan, F. (1994) Biochemistry 33, 6284-6294]. In the present, form, six contiguous subsites of the enzyme active site are occupied by, the carbohydrate ligand; the structural data indicate that the binding, site is capable of holding more than the five glucose units of the scheme, proposed through kinetic studies. A monosaccharide ring bridging two, protein molecules related by the crystal packing is located on the, surface, at a distance of 2.0 nm from the reducing end of the inhibitor, ligand; the symmetry-related glucose ring in the crystal lattice is found, 1.5 nm away from the non-reducing end of the inhibitor ligand.
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<StructureSection load='1ose' size='340' side='right'caption='[[1ose]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ose]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OSE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OSE FirstGlance]. <br>
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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]] 2.3&#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=AC1:6-METHYL-5-(4,5,6-TRIHYDROXY-3-HYDROXYMETHYL-CYCLOHEX-2-ENYLAMINO)-TETRAHYDRO-PYRAN-2,3,4-TRIOL'>AC1</scene>, <scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr>
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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=1ose FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ose OCA], [https://pdbe.org/1ose PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ose RCSB], [https://www.ebi.ac.uk/pdbsum/1ose PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ose ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AMYP_PIG AMYP_PIG]
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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/os/1ose_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=1ose ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1OSE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with GLC, CL and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Alpha-amylase Alpha-amylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.1 3.2.1.1] Structure known Active Sites: AS1, AS2, AS3, AS4, AS5, CAL and CLO. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OSE OCA].
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*[[Amylase 3D structures|Amylase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structure of pig pancreatic alpha-amylase isoenzyme II, in complex with the carbohydrate inhibitor acarbose., Gilles C, Astier JP, Marchis-Mouren G, Cambillau C, Payan F, Eur J Biochem. 1996 Jun 1;238(2):561-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8681972 8681972]
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[[Category: Large Structures]]
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[[Category: Alpha-amylase]]
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[[Category: Single protein]]
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[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
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[[Category: Gilles, C.]]
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[[Category: Gilles C]]
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[[Category: Payan, F.]]
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[[Category: Payan F]]
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[[Category: CA]]
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[[Category: CL]]
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[[Category: GLC]]
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[[Category: acarbose]]
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[[Category: alpha-amylase]]
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[[Category: hydrolase]]
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[[Category: hydrolase (o-glycosyl)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 16:58:47 2007''
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Current revision

Porcine pancreatic alpha-amylase complexed with acarbose

PDB ID 1ose

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