1bf2
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<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> | <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> | ||
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| - | <tr id=' | + | <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> |
<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> | <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> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ISOA_PSEAY ISOA_PSEAY] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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]. | </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]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | 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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| - | 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:9719642<ref>PMID:9719642</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1bf2" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Isoamylase]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Pseudomonas amyloderamosa]] | [[Category: Pseudomonas amyloderamosa]] | ||
| - | [[Category: Katsuya | + | [[Category: Katsuya Y]] |
| - | [[Category: Kubota | + | [[Category: Kubota M]] |
| - | [[Category: Matsuura | + | [[Category: Matsuura Y]] |
| - | [[Category: Mezaki | + | [[Category: Mezaki Y]] |
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Revision as of 15:32, 13 March 2024
STRUCTURE OF PSEUDOMONAS ISOAMYLASE
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