1ktw
From Proteopedia
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- | [[Image:1ktw.gif|left|200px]] | + | [[Image:1ktw.gif|left|200px]] |
- | + | ||
- | '''IOTA-CARRAGEENASE COMPLEXED TO IOTA-CARRAGEENAN FRAGMENTS''' | + | {{Structure |
+ | |PDB= 1ktw |SIZE=350|CAPTION= <scene name='initialview01'>1ktw</scene>, resolution 2.00Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene> and <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene> | ||
+ | |ACTIVITY= [http://en.wikipedia.org/wiki/Iota-carrageenase Iota-carrageenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.157 3.2.1.157] | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''IOTA-CARRAGEENASE COMPLEXED TO IOTA-CARRAGEENAN FRAGMENTS''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1KTW is a [ | + | 1KTW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Alteromonas_sp._atcc_43554 Alteromonas sp. atcc 43554]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KTW OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/14623184 14623184] |
[[Category: Alteromonas sp. atcc 43554]] | [[Category: Alteromonas sp. atcc 43554]] | ||
[[Category: Iota-carrageenase]] | [[Category: Iota-carrageenase]] | ||
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[[Category: iota-carrageenan double helix degradation]] | [[Category: iota-carrageenan double helix degradation]] | ||
- | ''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 12:22:05 2008'' |
Revision as of 10:22, 20 March 2008
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, resolution 2.00Å | |||||||
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Ligands: | , and | ||||||
Activity: | Iota-carrageenase, with EC number 3.2.1.157 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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.
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
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