From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1ktw.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1ktw.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1ktw| PDB=1ktw | SCENE= }} | | {{STRUCTURE_1ktw| PDB=1ktw | SCENE= }} |
| | | | |
| - | '''IOTA-CARRAGEENASE COMPLEXED TO IOTA-CARRAGEENAN FRAGMENTS'''
| + | ===IOTA-CARRAGEENASE COMPLEXED TO IOTA-CARRAGEENAN FRAGMENTS=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | iota-Carrageenans are sulfated 1,3-alpha-1,4-beta-galactans from the cell walls of red algae, which auto-associate into crystalline fibers made of aggregates of double-stranded helices. iota-Carrageenases, which constitute family 82 of glycoside hydrolases, fold into a right-handed beta-helix. Here, the structure of Alteromonas fortis iota-carrageenase bound to iota-carrageenan fragments was solved at 2.0A resolution (PDB 1KTW). The enzyme holds a iota-carrageenan tetrasaccharide (subsites +1 to +4) and a disaccharide (subsites -3, -4), thus providing the first direct determination of a 3D structure of iota-carrageenan. Electrostatic interactions between basic protein residues and the sulfate substituents of the polysaccharide chain dominate iota-carrageenan recognition. Glu245 and Asp247 are the proton donor and the base catalyst, respectively. C-terminal domain A, which was highly flexible in the native enzyme structure, adopts a alpha/beta-fold, also found in DNA/RNA-binding domains. In the substrate-enzyme complex, this polyanion-binding module shifts toward the beta-helix groove, forming a tunnel. Thus, from an open conformation which allows for the initial endo-attack of iota-carrageenan chains, the enzyme switches to a closed-tunnel form, consistent with its highly processive character, as seen from the electron-microscopy analysis of the degradation of iota-carrageenan fibers.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_14623184}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 14623184 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_14623184}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 28: |
Line 32: |
| | [[Category: Hydrolase]] | | [[Category: Hydrolase]] |
| | [[Category: Iota-carrageenan double helix degradation]] | | [[Category: Iota-carrageenan double helix degradation]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:10:05 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:59:46 2008'' |
Revision as of 07:59, 2 July 2008
Template:STRUCTURE 1ktw
IOTA-CARRAGEENASE COMPLEXED TO IOTA-CARRAGEENAN FRAGMENTS
Template:ABSTRACT PUBMED 14623184
About this Structure
1KTW is a Single protein structure of sequence from Alteromonas sp. atcc 43554. Full crystallographic information is available from OCA.
Reference
The structural bases of the processive degradation of iota-carrageenan, a main cell wall polysaccharide of red algae., Michel G, Helbert W, Kahn R, Dideberg O, Kloareg B, J Mol Biol. 2003 Nov 28;334(3):421-33. PMID:14623184
Page seeded by OCA on Wed Jul 2 10:59:46 2008
