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| | <StructureSection load='1ktw' size='340' side='right'caption='[[1ktw]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='1ktw' size='340' side='right'caption='[[1ktw]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1ktw]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KTW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KTW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1ktw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Alteromonas_macleodii Alteromonas macleodii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KTW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KTW FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=DGS:3,6-ANHYDRO-D-GALACTOSE-2-SULFATE'>DGS</scene>, <scene name='pdbligand=G4S:4-O-SULFO-BETA-D-GALACTOPYRANOSE'>G4S</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1h80|1h80]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DGS:3,6-ANHYDRO-D-GALACTOSE-2-SULFATE'>DGS</scene>, <scene name='pdbligand=G4S:4-O-SULFO-BETA-D-GALACTOPYRANOSE'>G4S</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Iota-carrageenase Iota-carrageenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.157 3.2.1.157] </span></td></tr>
| + | |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ktw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ktw OCA], [https://pdbe.org/1ktw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ktw RCSB], [https://www.ebi.ac.uk/pdbsum/1ktw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ktw ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ktw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ktw OCA], [https://pdbe.org/1ktw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ktw RCSB], [https://www.ebi.ac.uk/pdbsum/1ktw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ktw ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/CGIA_ALTMA CGIA_ALTMA] Hydrolyzes iota-carrageenans, sulfated 1,3-alpha-1,4-beta galactans from red algal cell walls, with an inversion of anomeric configuration. Also active against hybrid iota-/nu-carrageenan, not active against kappa- or lambda-carrageenans.[UniProtKB:Q9F284]<ref>PMID:10934194</ref> <ref>PMID:20227066</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Iota-carrageenase]] | + | [[Category: Alteromonas macleodii]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Dideberg, O]] | + | [[Category: Dideberg O]] |
| - | [[Category: Kahn, R]] | + | [[Category: Kahn R]] |
| - | [[Category: Michel, G]] | + | [[Category: Michel G]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Iota-carrageenan double helix degradation]]
| + | |
| Structural highlights
1ktw is a 2 chain structure with sequence from Alteromonas macleodii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
CGIA_ALTMA Hydrolyzes iota-carrageenans, sulfated 1,3-alpha-1,4-beta galactans from red algal cell walls, with an inversion of anomeric configuration. Also active against hybrid iota-/nu-carrageenan, not active against kappa- or lambda-carrageenans.[UniProtKB:Q9F284][1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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 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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Barbeyron T, Michel G, Potin P, Henrissat B, Kloareg B. iota-Carrageenases constitute a novel family of glycoside hydrolases, unrelated to that of kappa-carrageenases. J Biol Chem. 2000 Nov 10;275(45):35499-505. PMID:10934194 doi:http://dx.doi.org/10.1074/jbc.M003404200
- ↑ Jouanneau D, Boulenguer P, Mazoyer J, Helbert W. Enzymatic degradation of hybrid iota-/nu-carrageenan by Alteromonas fortis iota-carrageenase. Carbohydr Res. 2010 May 7;345(7):934-40. doi: 10.1016/j.carres.2010.02.014. Epub , 2010 Feb 19. PMID:20227066 doi:http://dx.doi.org/10.1016/j.carres.2010.02.014
- ↑ Michel G, Helbert W, Kahn R, Dideberg O, Kloareg B. The structural bases of the processive degradation of iota-carrageenan, a main cell wall polysaccharide of red algae. J Mol Biol. 2003 Nov 28;334(3):421-33. PMID:14623184
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