1wl7

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(New page: 200px<br /><applet load="1wl7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wl7, resolution 1.90&Aring;" /> '''Structure of the the...)
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[[Image:1wl7.gif|left|200px]]<br /><applet load="1wl7" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1wl7, resolution 1.90&Aring;" />
 
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'''Structure of the thermostable arabinanase'''<br />
 
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==Overview==
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==Structure of the thermostable arabinanase==
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The crystal structure of a thermostable endo-1,5-alpha-L-arabinanase, ABN-TS, from Bacillus thermodenitrificans TS-3 was determined at 1.9 A to, an R-factor of 18.3% and an R-free-factor of 22.5%. The enzyme molecule, has a five-bladed beta-propeller fold. The substrate-binding cleft formed, across one face of the propeller is open on both sides to allow random, binding of several sugar units in the polymeric substrate arabinan. The, beta-propeller fold is stabilized through a ring closure. ABN-TS exhibits, a new closure-mode involving residues in the N-terminal region: Phe7 to, Gly21 exhibit hydrogen bonds and hydrophobic interactions with the first, and last blades, and Phe4 links the second and third blades through a, hydrogen bond and an aromatic stacking interaction, respectively. The role, of the N-terminal region in the thermostability was confirmed with a, mutant lacking 16 amino acid residues from the N-terminus of ABN-TS.
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<StructureSection load='1wl7' size='340' side='right'caption='[[1wl7]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1wl7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_thermodenitrificans Geobacillus thermodenitrificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WL7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WL7 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]] 1.9&#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=1wl7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wl7 OCA], [https://pdbe.org/1wl7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wl7 RCSB], [https://www.ebi.ac.uk/pdbsum/1wl7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wl7 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/IABN_GEOTD IABN_GEOTD] Involved in the degradation of arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes the cleavage of endo alpha-(1->5)-L-arabinofuranosyl residues in debranched arabinan.<ref>PMID:11999422</ref>
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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/wl/1wl7_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1wl7 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 crystal structure of a thermostable endo-1,5-alpha-L-arabinanase, ABN-TS, from Bacillus thermodenitrificans TS-3 was determined at 1.9 A to an R-factor of 18.3% and an R-free-factor of 22.5%. The enzyme molecule has a five-bladed beta-propeller fold. The substrate-binding cleft formed across one face of the propeller is open on both sides to allow random binding of several sugar units in the polymeric substrate arabinan. The beta-propeller fold is stabilized through a ring closure. ABN-TS exhibits a new closure-mode involving residues in the N-terminal region: Phe7 to Gly21 exhibit hydrogen bonds and hydrophobic interactions with the first and last blades, and Phe4 links the second and third blades through a hydrogen bond and an aromatic stacking interaction, respectively. The role of the N-terminal region in the thermostability was confirmed with a mutant lacking 16 amino acid residues from the N-terminus of ABN-TS.
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==About this Structure==
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Structural basis for thermostability of endo-1,5-alpha-L-arabinanase from Bacillus thermodenitrificans TS-3.,Yamaguchi A, Tada T, Wada K, Nakaniwa T, Kitatani T, Sogabe Y, Takao M, Sakai T, Nishimura K J Biochem. 2005 May;137(5):587-92. PMID:15944411<ref>PMID:15944411</ref>
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1WL7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_thermodenitrificans Geobacillus thermodenitrificans] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Arabinan_endo-1,5-alpha-L-arabinosidase Arabinan endo-1,5-alpha-L-arabinosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.99 3.2.1.99] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WL7 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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Structural basis for thermostability of endo-1,5-alpha-L-arabinanase from Bacillus thermodenitrificans TS-3., Yamaguchi A, Tada T, Wada K, Nakaniwa T, Kitatani T, Sogabe Y, Takao M, Sakai T, Nishimura K, J Biochem (Tokyo). 2005 May;137(5):587-92. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15944411 15944411]
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</div>
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[[Category: Arabinan endo-1,5-alpha-L-arabinosidase]]
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<div class="pdbe-citations 1wl7" style="background-color:#fffaf0;"></div>
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[[Category: Geobacillus thermodenitrificans]]
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[[Category: Single protein]]
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[[Category: Kitatani, T.]]
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[[Category: Nakaniwa, T.]]
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[[Category: Tada, T.]]
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[[Category: Yamaguchi, A.]]
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[[Category: CA]]
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[[Category: abn-ts]]
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[[Category: arabinanase]]
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[[Category: bacillus]]
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[[Category: glycoside hydrolase]]
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[[Category: thermostable enzyme]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 00:10:00 2007''
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==See Also==
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*[[Arabinanase 3D structures|Arabinanase 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: Geobacillus thermodenitrificans]]
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[[Category: Large Structures]]
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[[Category: Kitatani T]]
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[[Category: Nakaniwa T]]
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[[Category: Tada T]]
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[[Category: Yamaguchi A]]

Current revision

Structure of the thermostable arabinanase

PDB ID 1wl7

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