1ji2

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(New page: 200px<br /><applet load="1ji2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ji2, resolution 2.30&Aring;" /> '''Improved X-ray Struc...)
Current revision (13:24, 13 March 2024) (edit) (undo)
 
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[[Image:1ji2.jpg|left|200px]]<br /><applet load="1ji2" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ji2, resolution 2.30&Aring;" />
 
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'''Improved X-ray Structure of Thermoactinomyces vulgaris R-47 alpha-Amylase 2'''<br />
 
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==Overview==
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==Improved X-ray Structure of Thermoactinomyces vulgaris R-47 alpha-Amylase 2==
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The X-ray crystal structures of Thermoactinomyces vulgaris R-47, alpha-amylase 1 (TVAI) and alpha-amylase 2 (TVAII) have been determined at, 1.6 A and 2.3 A resolution, respectively. The structures of TVAI and TVAII, have been refined, R-factor of 0.182 (R(free)=0.206) and 0.179 (0.224), respectively, with good chemical geometries. Both TVAI and TVAII have four, domains, N, A, B and C, and all very similar in structure. However, there, are some differences in the structures between them. Domain N of TVAI, interacts strongly with domains A and B, giving a spherical shape, structure to the enzyme, while domain N of TVAII is isolated from the, other domains, which leads to the formation of a dimer. TVAI has three, bound Ca ions, whereas TVAII has only one. TVAI has eight extra loops, compared to TVAII, while TVAII has two extra loops compared to TVAI. TVAI, can hydrolyze substrates more efficiently than TVAII with a high molecular, mass such as starch, while TVAII is much more active against cyclodextrins, than TVAI and other alpha-amylases. A structural comparison of the active, sites has clearly revealed this difference in substrate specificity.
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<StructureSection load='1ji2' size='340' side='right'caption='[[1ji2]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ji2]] 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=1JI2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JI2 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]] 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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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ji2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ji2 OCA], [https://pdbe.org/1ji2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ji2 RCSB], [https://www.ebi.ac.uk/pdbsum/1ji2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ji2 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/ji/1ji2_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=1ji2 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1JI2 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 CA 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=1JI2 OCA].
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*[[Amylase 3D structures|Amylase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structures and structural comparison of Thermoactinomyces vulgaris R-47 alpha-amylase 1 (TVAI) at 1.6 A resolution and alpha-amylase 2 (TVAII) at 2.3 A resolution., Kamitori S, Abe A, Ohtaki A, Kaji A, Tonozuka T, Sakano Y, J Mol Biol. 2002 Apr 26;318(2):443-53. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12051850 12051850]
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[[Category: Large Structures]]
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[[Category: Neopullulanase]]
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[[Category: Single protein]]
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[[Category: Thermoactinomyces vulgaris]]
[[Category: Thermoactinomyces vulgaris]]
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[[Category: Abe, A.]]
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[[Category: Abe A]]
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[[Category: Kaji, A.]]
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[[Category: Kaji A]]
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[[Category: Kamitori, S.]]
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[[Category: Kamitori S]]
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[[Category: Ohtaki, A.]]
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[[Category: Ohtaki A]]
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[[Category: Sakano, Y.]]
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[[Category: Sakano Y]]
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[[Category: Tonozuka, T.]]
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[[Category: Tonozuka T]]
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[[Category: CA]]
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[[Category: beta/alpha barrel]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:16:57 2007''
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Current revision

Improved X-ray Structure of Thermoactinomyces vulgaris R-47 alpha-Amylase 2

PDB ID 1ji2

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