1jl8

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(New page: 200px<br /><applet load="1jl8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jl8, resolution 3.20&Aring;" /> '''Complex of alpha-amy...)
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[[Image:1jl8.jpg|left|200px]]<br /><applet load="1jl8" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1jl8, resolution 3.20&Aring;" />
 
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'''Complex of alpha-amylase II (TVA II) from Thermoactinomyces vulgaris R-47 with beta-cyclodextrin based on a co-crystallization with methyl beta-cyclodextrin'''<br />
 
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==Overview==
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==Complex of alpha-amylase II (TVA II) from Thermoactinomyces vulgaris R-47 with beta-cyclodextrin based on a co-crystallization with methyl beta-cyclodextrin==
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The structures of Thermoactinomyces vulgaris R-47 alpha-amylase II mutant, (d325nTVA II) complexed with substrate analogues, methyl beta-cyclodextrin, (m beta-CD) and maltohexaose (G6), were solved by X-ray diffraction at 3.2, A and 3.3 A resolution, respectively. In d325nTVA II-m beta-CD complex, the orientation and binding-position of beta-CD in TVA II were identical, to those in cyclodextin glucanotransferase (CGTase). The active site, residues were essentialy conserved, while there are no residues, corresponding to Tyr89, Phe183, and His233 of CGTase in TVA II. In, d325nTVA II-G6 complex, the electron density maps of two glucosyl units at, the non-reducing end were disordered and invisible. The four glucosyl, units of G6 were bound to TVA II as in CGTase, while the others were not, stacked and were probably flexible. The residues of TVA II corresponding, to Tyr89, Lys232, and His233 of CGTase were completely lacking. These, results suggest that the lack of the residues related to alpha-glucan and, CD-stacking causes the functional distinctions between CGTase and TVA II.
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<StructureSection load='1jl8' size='340' side='right'caption='[[1jl8]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1jl8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermoactinomyces_vulgaris Thermoactinomyces vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JL8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JL8 FirstGlance]. <br>
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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]] 3.2&#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=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900012:beta-cyclodextrin'>PRD_900012</scene></td></tr>
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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=1jl8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jl8 OCA], [https://pdbe.org/1jl8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jl8 RCSB], [https://www.ebi.ac.uk/pdbsum/1jl8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jl8 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/NEPU2_THEVU NEPU2_THEVU] Hydrolyzes pullulan efficiently but only a small amount of starch. Endohydrolysis of 1,4-alpha-glucosidic linkages in pullulan to form panose. Cleaves also (1-6)-alpha-glucosidic linkages to form maltotriose.
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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/jl/1jl8_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=1jl8 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The structures of Thermoactinomyces vulgaris R-47 alpha-amylase II mutant (d325nTVA II) complexed with substrate analogues, methyl beta-cyclodextrin (m beta-CD) and maltohexaose (G6), were solved by X-ray diffraction at 3.2 A and 3.3 A resolution, respectively. In d325nTVA II-m beta-CD complex, the orientation and binding-position of beta-CD in TVA II were identical to those in cyclodextin glucanotransferase (CGTase). The active site residues were essentialy conserved, while there are no residues corresponding to Tyr89, Phe183, and His233 of CGTase in TVA II. In d325nTVA II-G6 complex, the electron density maps of two glucosyl units at the non-reducing end were disordered and invisible. The four glucosyl units of G6 were bound to TVA II as in CGTase, while the others were not stacked and were probably flexible. The residues of TVA II corresponding to Tyr89, Lys232, and His233 of CGTase were completely lacking. These results suggest that the lack of the residues related to alpha-glucan and CD-stacking causes the functional distinctions between CGTase and TVA II.
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==About this Structure==
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Structures of Thermoactinomyces vulgaris R-47 alpha-amylase II complexed with substrate analogues.,Yokota T, Tonozuka T, Shimura Y, Ichikawa K, Kamitori S, Sakano Y Biosci Biotechnol Biochem. 2001 Mar;65(3):619-26. PMID:11330677<ref>PMID:11330677</ref>
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1JL8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermoactinomyces_vulgaris Thermoactinomyces vulgaris] with BCD as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Neopullulanase Neopullulanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.135 3.2.1.135] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JL8 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Structures of Thermoactinomyces vulgaris R-47 alpha-amylase II complexed with substrate analogues., Yokota T, Tonozuka T, Shimura Y, Ichikawa K, Kamitori S, Sakano Y, Biosci Biotechnol Biochem. 2001 Mar;65(3):619-26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11330677 11330677]
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</div>
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[[Category: Neopullulanase]]
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<div class="pdbe-citations 1jl8" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Thermoactinomyces vulgaris]]
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[[Category: Ichikawa, K.]]
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[[Category: Kamitori, S.]]
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[[Category: Sakano, Y.]]
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[[Category: Shimura, Y.]]
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[[Category: Tonozuka, T.]]
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[[Category: Yokota, T.]]
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[[Category: BCD]]
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[[Category: beta-cyclodextrin]]
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[[Category: cyclodextrin]]
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[[Category: methyl beta-cyclodextrin]]
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[[Category: neopullulanase]]
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[[Category: pullulan]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:21:43 2007''
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==See Also==
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*[[Amylase 3D structures|Amylase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Thermoactinomyces vulgaris]]
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[[Category: Ichikawa K]]
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[[Category: Kamitori S]]
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[[Category: Sakano Y]]
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[[Category: Shimura Y]]
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[[Category: Tonozuka T]]
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[[Category: Yokota T]]

Current revision

Complex of alpha-amylase II (TVA II) from Thermoactinomyces vulgaris R-47 with beta-cyclodextrin based on a co-crystallization with methyl beta-cyclodextrin

PDB ID 1jl8

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