1wl7: Difference between revisions
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<StructureSection load='1wl7' size='340' side='right'caption='[[1wl7]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='1wl7' size='340' side='right'caption='[[1wl7]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1wl7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <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> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | ||
<tr id=' | <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> | ||
<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> | <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> | ||
</table> | </table> | ||
== Function == | |||
[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> | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Geobacillus thermodenitrificans]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Kitatani | [[Category: Kitatani T]] | ||
[[Category: Nakaniwa | [[Category: Nakaniwa T]] | ||
[[Category: Tada | [[Category: Tada T]] | ||
[[Category: Yamaguchi | [[Category: Yamaguchi A]] | ||
Revision as of 10:56, 25 October 2023
Structure of the thermostable arabinanaseStructure of the thermostable arabinanase
Structural highlights
FunctionIABN_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.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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