First time at Proteopedia? Click on the green links: they change the 3D image. Click and drag the molecules. Proteopedia is a 3D, interactive encyclopedia of proteins, RNA, DNA and other molecules. With a free user account, you can edit pages in Proteopedia. Visit the Main Page to learn more.

1bf2

From Proteopedia

Jump to: navigation, search


1bf2, resolution 2.00Å ()
Ligands:
Activity: Isoamylase, with EC number 3.2.1.68
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml



STRUCTURE OF PSEUDOMONAS ISOAMYLASE

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.

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

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1bf2 is a 1 chain structure with sequence from Pseudomonas amyloderamosa. Full crystallographic information is available from OCA.

Reference

  • Katsuya Y, Mezaki Y, Kubota M, Matsuura Y. Three-dimensional structure of Pseudomonas isoamylase at 2.2 A resolution. J Mol Biol. 1998 Sep 4;281(5):885-97. PMID:9719642 doi:10.1006/jmbi.1998.1992

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools