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1cxe

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[[Image:1cxe.gif|left|200px]]
 
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==COMPLEX OF CGTASE WITH MALTOTETRAOSE AT ROOM TEMPERATURE AND PH 9.1 BASED ON DIFFRACTION DATA OF A CRYSTAL SOAKED WITH ALPHA-CYCLODEXTRIN==
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The line below this paragraph, containing "STRUCTURE_1cxe", creates the "Structure Box" on the page.
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<StructureSection load='1cxe' size='340' side='right'caption='[[1cxe]], [[Resolution|resolution]] 2.10&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'>[[1cxe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Niallia_circulans Niallia circulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CXE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CXE 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]] 2.1&#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>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</scene>, <scene name='pdbligand=PRD_900010:alpha-maltotetraose'>PRD_900010</scene></td></tr>
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{{STRUCTURE_1cxe| PDB=1cxe | 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=1cxe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cxe OCA], [https://pdbe.org/1cxe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cxe RCSB], [https://www.ebi.ac.uk/pdbsum/1cxe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cxe ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CDGT2_NIACI CDGT2_NIACI]
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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/cx/1cxe_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=1cxe ConSurf].
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<div style="clear:both"></div>
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'''COMPLEX OF CGTASE WITH MALTOTETRAOSE AT ROOM TEMPERATURE AND PH 9.1 BASED ON DIFFRACTION DATA OF A CRYSTAL SOAKED WITH ALPHA-CYCLODEXTRIN'''
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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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Asp-229, Glu-257, and Asp-328 constitute the catalytic residues in cyclodextrin glycosyl transferase from Bacillus circulans strain 251. Via site-directed mutagenesis constructed D229N, E257Q, and D328N mutant proteins showed a 4,000-60,000-fold reduction of cyclization activity. A D229N/E257Q double mutant showed a 700,000-fold reduction and was crystallized for use in soaking experiments with alpha-cyclodextrin. Crystal structures were determined of wild type CGTase soaked at elevated pH with alpha-cyclodextrin (resolution, 2.1 A) and maltoheptaose (2.4 A). In addition, structures at cryogenic temperature were solved of the unliganded enzyme (2.2 A) and of the D229N/E257Q mutant after soaking with alpha-cyclodextrin (2.6 A). In the crystals soaked in alpha-cyclodextrin and maltoheptaose, a maltotetraose molecule is observed to bind in the active site. Residue 229 is at hydrogen bonding distance from the C-6 hydroxyl group of the sugar, which after cleavage will contain the new reducing end. In the D229N/E257Q double mutant structure, two alpha-cyclodextrins are observed to replace two maltoses at the E-domain, thus providing structural information on product inhibition via binding to the enzyme's raw starch binding domain.
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[[Category: Large Structures]]
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[[Category: Niallia circulans]]
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==About this Structure==
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[[Category: Dijkstra BW]]
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1CXE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_circulans Bacillus circulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CXE OCA].
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[[Category: Knegtel RMA]]
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[[Category: Strokopytov BV]]
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==Reference==
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Crystallographic studies of the interaction of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 with natural substrates and products., Knegtel RM, Strokopytov B, Penninga D, Faber OG, Rozeboom HJ, Kalk KH, Dijkhuizen L, Dijkstra BW, J Biol Chem. 1995 Dec 8;270(49):29256-64. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7493956 7493956]
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[[Category: Bacillus circulans]]
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[[Category: Cyclomaltodextrin glucanotransferase]]
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[[Category: Single protein]]
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[[Category: Dijkstra, B W.]]
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[[Category: Knegtel, R M.A.]]
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[[Category: Strokopytov, B V.]]
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[[Category: Glycosyltransferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:13:02 2008''
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Current revision

COMPLEX OF CGTASE WITH MALTOTETRAOSE AT ROOM TEMPERATURE AND PH 9.1 BASED ON DIFFRACTION DATA OF A CRYSTAL SOAKED WITH ALPHA-CYCLODEXTRIN

PDB ID 1cxe

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