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1ciu

From Proteopedia

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[[Image:1ciu.gif|left|200px]]
 
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==THERMOSTABLE CGTASE FROM THERMOANAEROBACTERIUM THERMOSULFURIGENES EM1 AT PH 8.0.==
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The line below this paragraph, containing "STRUCTURE_1ciu", creates the "Structure Box" on the page.
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<StructureSection load='1ciu' size='340' side='right'caption='[[1ciu]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1ciu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermoanaerobacterium_thermosulfurigenes Thermoanaerobacterium thermosulfurigenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CIU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CIU FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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{{STRUCTURE_1ciu| PDB=1ciu | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ciu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ciu OCA], [https://pdbe.org/1ciu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ciu RCSB], [https://www.ebi.ac.uk/pdbsum/1ciu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ciu ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CDGT_THETU CDGT_THETU] Degrades starch to alpha-, beta-, and gamma-cyclodextrins, as well as linear sugars.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ci/1ciu_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ciu ConSurf].
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<div style="clear:both"></div>
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'''THERMOSTABLE CGTASE FROM THERMOANAEROBACTERIUM THERMOSULFURIGENES EM1 AT PH 8.0.'''
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==See Also==
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*[[Glycosyltransferase 3D structures|Glycosyltransferase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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The crystal structure of the cyclodextrin glycosyltransferase (CGTase) from the thermophilic microorganism Thermoanaerobacterium thermosulfurigenes EM1 has been elucidated at 2.3 A resolution. The final model consists of all 683 amino acid residues, two calcium ions and 343 water molecules, and has a crystallographic R-factor of 17.9% (Rfree 24.9%) with excellent stereochemistry. The overall fold of the enzyme is highly similar to that reported for mesophilic CGTases and differences are observed only at surface loop regions. Closer inspection of these loop regions and comparison with other CGTase structures reveals that especially loops 88-95, 335-339 and 534-539 possibly contribute with novel hydrogen bonds and apolar contacts to the stabilization of the enzyme. Other structural features that might confer thermostability to the T. thermosulfurigenes EM1 CGTase are the introduction of five new salt-bridges and three Gly to Ala/Pro substitutions. The abundance of Ser, Thr and Tyr residues near the active site and oligosaccharide binding sites might explain the increased thermostability of CGTase in the presence of starch, by allowing amylose chains to bind non-specifically to the protein. Additional stabilization of the A/E domain interface through apolar contacts involves residues Phe273 and Tyr187. No additional or improved calcium binding is observed in the structure, suggesting that the observed stabilization in the presence of calcium ions is caused by the reduced exchange of calcium from the protein to the solvent, rendering it less susceptible to unfolding. The 50% decrease in cyclization activity of the T. thermosulfurigenes EM1 CGTase compared with that of B. circulans strain 251 appears to be caused by the changes in the conformation and amino acid composition of the 88-95 loop. In the T. thermosulfurigenes EM1 CGTase there is no residue homologous to Tyr89, which was observed to take part in stacking interactions with bound substrate in the case of the B. circulans strain 251 CGTase. The lack of this interaction in the enzyme-substrate complex is expected to destabilize bound substrates prior to cyclization. Apparently, some catalytic functionality of CGTase has been sacrificed for the sake of structural stability by modifying loop regions near the active site.
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[[Category: Large Structures]]
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==About this Structure==
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1CIU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermoanaerobacterium_thermosulfurigenes Thermoanaerobacterium thermosulfurigenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CIU OCA].
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==Reference==
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Crystal structure at 2.3 A resolution and revised nucleotide sequence of the thermostable cyclodextrin glycosyltransferase from Thermonanaerobacterium thermosulfurigenes EM1., Knegtel RM, Wind RD, Rozeboom HJ, Kalk KH, Buitelaar RM, Dijkhuizen L, Dijkstra BW, J Mol Biol. 1996 Mar 1;256(3):611-22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8604143 8604143]
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[[Category: Cyclomaltodextrin glucanotransferase]]
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[[Category: Single protein]]
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[[Category: Thermoanaerobacterium thermosulfurigenes]]
[[Category: Thermoanaerobacterium thermosulfurigenes]]
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[[Category: Dijkstra, B W.]]
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[[Category: Dijkstra BW]]
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[[Category: Knegtel, R M.A.]]
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[[Category: Knegtel RMA]]
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[[Category: Thermostable]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:46:43 2008''
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Current revision

THERMOSTABLE CGTASE FROM THERMOANAEROBACTERIUM THERMOSULFURIGENES EM1 AT PH 8.0.

PDB ID 1ciu

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