1bf2: Difference between revisions
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[[Image:1bf2.gif|left|200px]] | [[Image:1bf2.gif|left|200px]] | ||
'''STRUCTURE OF PSEUDOMONAS ISOAMYLASE''' | {{Structure | ||
|PDB= 1bf2 |SIZE=350|CAPTION= <scene name='initialview01'>1bf2</scene>, resolution 2.0Å | |||
|SITE= | |||
|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] | |||
|GENE= | |||
}} | |||
'''STRUCTURE OF PSEUDOMONAS ISOAMYLASE''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1BF2 is a [ | 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]. | ||
==Reference== | ==Reference== | ||
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:// | 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] | ||
[[Category: Isoamylase]] | [[Category: Isoamylase]] | ||
[[Category: Pseudomonas amyloderamosa]] | [[Category: Pseudomonas amyloderamosa]] | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:10:08 2008'' | ||
Revision as of 11:10, 20 March 2008
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| , resolution 2.0Å | |||||||
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| Ligands: | |||||||
| Activity: | Isoamylase, with EC number 3.2.1.68 | ||||||
| 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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