This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1bf2

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
[[Image:1bf2.gif|left|200px]]
[[Image:1bf2.gif|left|200px]]
-
{{Structure
+
<!--
-
|PDB= 1bf2 |SIZE=350|CAPTION= <scene name='initialview01'>1bf2</scene>, resolution 2.0&Aring;
+
The line below this paragraph, containing "STRUCTURE_1bf2", creates the "Structure Box" on the page.
-
|SITE=
+
You may change the PDB parameter (which sets the PDB file loaded into the applet)
-
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>
+
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-
|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>
+
or leave the SCENE parameter empty for the default display.
-
|GENE=
+
-->
-
|DOMAIN=
+
{{STRUCTURE_1bf2| PDB=1bf2 | SCENE= }}
-
|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>
+
-
}}
+
'''STRUCTURE OF PSEUDOMONAS ISOAMYLASE'''
'''STRUCTURE OF PSEUDOMONAS ISOAMYLASE'''
Line 30: Line 27:
[[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 Fri May 2 11:25:55 2008''
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:59:37 2008''
+

Revision as of 08:25, 2 May 2008

Template:STRUCTURE 1bf2

STRUCTURE OF PSEUDOMONAS ISOAMYLASE


Overview

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 Structure

1BF2 is a Single protein structure of sequence from Pseudomonas amyloderamosa. Full crystallographic information is available from OCA.

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:9719642 Page seeded by OCA on Fri May 2 11:25:55 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools