1bf2: Difference between revisions
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|PDB= 1bf2 |SIZE=350|CAPTION= <scene name='initialview01'>1bf2</scene>, resolution 2.0Å | |PDB= 1bf2 |SIZE=350|CAPTION= <scene name='initialview01'>1bf2</scene>, resolution 2.0Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Isoamylase Isoamylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.68 3.2.1.68] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Isoamylase Isoamylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.68 3.2.1.68] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bf2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bf2 OCA], [http://www.ebi.ac.uk/pdbsum/1bf2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bf2 RCSB]</span> | |||
}} | }} | ||
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[[Category: Matsuura, Y.]] | [[Category: Matsuura, Y.]] | ||
[[Category: Mezaki, Y.]] | [[Category: Mezaki, Y.]] | ||
[[Category: debranching enzyme]] | [[Category: debranching enzyme]] | ||
[[Category: glycosidase]] | [[Category: glycosidase]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:59:37 2008'' | ||
Revision as of 18:59, 30 March 2008
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| , resolution 2.0Å | |||||||
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| Ligands: | |||||||
| Activity: | Isoamylase, with EC number 3.2.1.68 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF PSEUDOMONAS ISOAMYLASE
OverviewOverview
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.
About this StructureAbout this Structure
1BF2 is a Single protein structure of sequence from Pseudomonas amyloderamosa. Full crystallographic information is available from OCA.
ReferenceReference
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
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