2x8t: Difference between revisions
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< | ==Crystal Structure of the Abn2 H318A mutant== | ||
<StructureSection load='2x8t' size='340' side='right'caption='[[2x8t]], [[Resolution|resolution]] 1.79Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2x8t]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X8T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X8T FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.79Å</td></tr> | |||
-- | <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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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=2x8t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x8t OCA], [https://pdbe.org/2x8t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x8t RCSB], [https://www.ebi.ac.uk/pdbsum/2x8t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x8t ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/EABN2_BACSU EABN2_BACSU] Involved in the degradation of arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes the internal cleavage of alpha-(1->5)-L-arabinofuranosyl residues of the alpha-1,5-L-arabinan to produce arabino-oligosaccharides and L-arabinose. It is also active toward linear branched sugar beet arabinan, and pectin from apple.<ref>PMID:18408032</ref> <ref>PMID:20883454</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Endo-1,5-alpha-l-arabinanases are glycosyl hydrolases that are able to cleave the glycosidic bonds of alpha-1,5-l-arabinan, releasing arabino-oligosaccharides and l-arabinose. Two extracellular endo-1,5-alpha-l-arabinanases have been isolated from Bacillus subtilis, BsArb43A and BsArb43B (formally named AbnA and Abn2, respectively). BsArb43B shows low sequence identity with previously characterized 1,5-alpha-l-arabinanases and is a much larger enzyme. Here we describe the 3D structure of native BsArb43B, biochemical and structure characterization of two BsArb43B mutant proteins (H318A and D171A), and the 3D structure of the BsArb43B D171A mutant enzyme in complex with arabinohexose. The 3D structure of BsArb43B is different from that of other structurally characterized endo-1,5-alpha-l-arabinanases, as it comprises two domains, an N-terminal catalytic domain, with a 3D fold similar to that observed for other endo-1,5-alpha-l-arabinanases, and an additional C-terminal domain. Moreover, this work also provides experimental evidence for the presence of a cluster containing a calcium ion in the catalytic domain, and the importance of this calcium ion in the enzymatic mechanism of BsArb43B. | |||
New evidence for the role of calcium in the glycosidase reaction of GH43 arabinanases.,De Sanctis D, Inacio JM, Lindley PF, De Sa-Nogueira I, Bento I FEBS J. 2010 Sep 10. doi: 10.1111/j.1742-4658.2010.07870.x. PMID:20883454<ref>PMID:20883454</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2x8t" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Arabinanase 3D structures|Arabinanase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
[[ | |||
== | |||
< | |||
[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Bento I]] | ||
[[Category: Inacio | [[Category: Inacio JM]] | ||
[[Category: Lindley | [[Category: Lindley PF]] | ||
[[Category: Sa-Nogueira | [[Category: De Sa-Nogueira I]] | ||
[[Category: DeSanctis D]] | |||
Latest revision as of 13:26, 20 December 2023
Crystal Structure of the Abn2 H318A mutantCrystal Structure of the Abn2 H318A mutant
Structural highlights
FunctionEABN2_BACSU Involved in the degradation of arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes the internal cleavage of alpha-(1->5)-L-arabinofuranosyl residues of the alpha-1,5-L-arabinan to produce arabino-oligosaccharides and L-arabinose. It is also active toward linear branched sugar beet arabinan, and pectin from apple.[1] [2] Publication Abstract from PubMedEndo-1,5-alpha-l-arabinanases are glycosyl hydrolases that are able to cleave the glycosidic bonds of alpha-1,5-l-arabinan, releasing arabino-oligosaccharides and l-arabinose. Two extracellular endo-1,5-alpha-l-arabinanases have been isolated from Bacillus subtilis, BsArb43A and BsArb43B (formally named AbnA and Abn2, respectively). BsArb43B shows low sequence identity with previously characterized 1,5-alpha-l-arabinanases and is a much larger enzyme. Here we describe the 3D structure of native BsArb43B, biochemical and structure characterization of two BsArb43B mutant proteins (H318A and D171A), and the 3D structure of the BsArb43B D171A mutant enzyme in complex with arabinohexose. The 3D structure of BsArb43B is different from that of other structurally characterized endo-1,5-alpha-l-arabinanases, as it comprises two domains, an N-terminal catalytic domain, with a 3D fold similar to that observed for other endo-1,5-alpha-l-arabinanases, and an additional C-terminal domain. Moreover, this work also provides experimental evidence for the presence of a cluster containing a calcium ion in the catalytic domain, and the importance of this calcium ion in the enzymatic mechanism of BsArb43B. New evidence for the role of calcium in the glycosidase reaction of GH43 arabinanases.,De Sanctis D, Inacio JM, Lindley PF, De Sa-Nogueira I, Bento I FEBS J. 2010 Sep 10. doi: 10.1111/j.1742-4658.2010.07870.x. PMID:20883454[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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