From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1bf2.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1bf2.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1bf2| PDB=1bf2 | SCENE= }} | | {{STRUCTURE_1bf2| PDB=1bf2 | SCENE= }} |
| | | | |
| - | '''STRUCTURE OF PSEUDOMONAS ISOAMYLASE'''
| + | ===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. | + | The line below this paragraph, {{ABSTRACT_PUBMED_9719642}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 9719642 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_9719642}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 30: |
Line 34: |
| | [[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 Mon Jun 30 19:00:45 2008'' |
Revision as of 16:00, 30 June 2008
Template:STRUCTURE 1bf2
STRUCTURE OF PSEUDOMONAS ISOAMYLASE
Template:ABSTRACT PUBMED 9719642
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 Mon Jun 30 19:00:45 2008
