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1bf2

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[[Image:1bf2.gif|left|200px]]
 
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==STRUCTURE OF PSEUDOMONAS ISOAMYLASE==
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The line below this paragraph, containing "STRUCTURE_1bf2", creates the "Structure Box" on the page.
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<StructureSection load='1bf2' size='340' side='right'caption='[[1bf2]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1bf2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_amyloderamosa Pseudomonas amyloderamosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BF2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BF2 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&#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=CA:CALCIUM+ION'>CA</scene></td></tr>
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{{STRUCTURE_1bf2| PDB=1bf2 | SCENE= }}
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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=1bf2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bf2 OCA], [https://pdbe.org/1bf2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bf2 RCSB], [https://www.ebi.ac.uk/pdbsum/1bf2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bf2 ProSAT]</span></td></tr>
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</table>
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'''STRUCTURE OF PSEUDOMONAS ISOAMYLASE'''
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== Function ==
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[https://www.uniprot.org/uniprot/ISOA_PSEAY ISOA_PSEAY]
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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The three-dimensional structure of isoamylase from Pseudomonas amyloderamosa, which hydrolyzes alpha-1,6-glucosidic linkages of amylopectin and glycogen, has been determined by X-ray structure analysis. The enzyme has 750 amino acid residues and a molecular mass of 80 kDa, and it can be crystallized from ammonium sulfate solution. The structure was elucidated by the multiple isomorphous replacement method and refined at 2.2 A resolution, resulting in a final R-factor of 0.161 for significant reflections with a root-mean-square deviation from ideality in bond lengths of 0.009 A. The analysis revealed that in the N-terminal region, isoamylase has a novel extra domain that we call domain N, whose three-dimensional structure has not so far been reported. It has a (beta/alpha)8-barrel-type supersecondary structure in the catalytic domain common to the alpha-amylase family enzymes, though the barrel is incomplete, with a deletion of an alpha-helix between the fifth and sixth beta-strands. A long excursed region is present between the third beta-strand and the third alpha-helix of the barrel but, in contrast to the so-called domain B that has been identified in the other enzymes of alpha-amylase family, it cannot be considered to be an independent domain, because this loop forms a globular cluster together with the loop between the fourth beta-strand and the fourth alpha-helix. Isoamylase contains a bound calcium ion, but this is not in the same position as the conserved calcium ion that has been reported in other alpha-amylase family enzymes.
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Check<jmol>
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<jmolCheckbox>
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==About this Structure==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bf/1bf2_consurf.spt"</scriptWhenChecked>
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1BF2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_amyloderamosa Pseudomonas amyloderamosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BF2 OCA].
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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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==Reference==
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</jmolCheckbox>
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Three-dimensional structure of Pseudomonas isoamylase at 2.2 A resolution., Katsuya Y, Mezaki Y, Kubota M, Matsuura Y, J Mol Biol. 1998 Sep 4;281(5):885-97. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9719642 9719642]
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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=1bf2 ConSurf].
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[[Category: Isoamylase]]
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Pseudomonas amyloderamosa]]
[[Category: Pseudomonas amyloderamosa]]
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[[Category: Single protein]]
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[[Category: Katsuya Y]]
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[[Category: Katsuya, Y.]]
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[[Category: Kubota M]]
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[[Category: Kubota, M.]]
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[[Category: Matsuura Y]]
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[[Category: Matsuura, Y.]]
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[[Category: Mezaki Y]]
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[[Category: Mezaki, Y.]]
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[[Category: Debranching enzyme]]
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[[Category: Glycosidase]]
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[[Category: Hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:25:55 2008''
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Current revision

STRUCTURE OF PSEUDOMONAS ISOAMYLASE

PDB ID 1bf2

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