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| | <StructureSection load='2xn2' size='340' side='right'caption='[[2xn2]], [[Resolution|resolution]] 1.58Å' scene=''> | | <StructureSection load='2xn2' size='340' side='right'caption='[[2xn2]], [[Resolution|resolution]] 1.58Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2xn2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lacac Lacac]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XN2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XN2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2xn2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactobacillus_acidophilus_NCFM Lactobacillus acidophilus NCFM]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XN2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XN2 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.58Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SME:METHIONINE+SULFOXIDE'>SME</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=SME:METHIONINE+SULFOXIDE'>SME</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2xn0|2xn0]], [[2xn1|2xn1]]</div></td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Alpha-galactosidase Alpha-galactosidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.22 3.2.1.22] </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=2xn2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xn2 OCA], [https://pdbe.org/2xn2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xn2 RCSB], [https://www.ebi.ac.uk/pdbsum/2xn2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xn2 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=2xn2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xn2 OCA], [https://pdbe.org/2xn2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xn2 RCSB], [https://www.ebi.ac.uk/pdbsum/2xn2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xn2 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/MELA_LACAC MELA_LACAC] Hydrolyzes the short-chain alpha-galactosaccharide raffinose. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Alpha-galactosidase]] | + | [[Category: Lactobacillus acidophilus NCFM]] |
| - | [[Category: Lacac]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Fredslund, F]] | + | [[Category: Abou Hachem M]] |
| - | [[Category: Hachem, M Abou]] | + | [[Category: Fredslund F]] |
| - | [[Category: Larsen, R J]] | + | [[Category: Larsen RJ]] |
| - | [[Category: Leggio, L Lo]] | + | [[Category: Lo Leggio L]] |
| - | [[Category: Sorensen, P G]] | + | [[Category: Sorensen PG]] |
| - | [[Category: Svensson, B]] | + | [[Category: Svensson B]] |
| - | [[Category: Glycosidase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
MELA_LACAC Hydrolyzes the short-chain alpha-galactosaccharide raffinose.
Publication Abstract from PubMed
Lactobacillus acidophilus NCFM is a probiotic bacterium known for its beneficial effects on human health. The importance of alpha-galactosidases (alpha-Gals) for growth of probiotic organisms on oligosaccharides of the raffinose family present in many foods is increasingly recognized. Here, the crystal structure of alpha-Gal from L. acidophilus NCFM (LaMel36A) of glycoside hydrolase (GH) family 36 (GH36) is determined by single-wavelength anomalous dispersion. In addition, a 1.58-A-resolution crystallographic complex with alpha-d-galactose at substrate binding subsite -1 was determined. LaMel36A has a large N-terminal twisted beta-sandwich domain, connected by a long alpha-helix to the catalytic (beta/alpha)(8)-barrel domain, and a C-terminal beta-sheet domain. Four identical monomers form a tightly packed tetramer where three monomers contribute to the structural integrity of the active site in each monomer. Structural comparison of LaMel36A with the monomeric Thermotoga maritima alpha-Gal (TmGal36A) reveals that O2 of alpha-d-galactose in LaMel36A interacts with a backbone nitrogen in a glycine-rich loop of the catalytic domain, whereas the corresponding atom in TmGal36A is from a tryptophan side chain belonging to the N-terminal domain. Thus, two distinctly different structural motifs participate in substrate recognition. The tetrameric LaMel36A furthermore has a much deeper active site than the monomeric TmGal36A, which possibly modulates substrate specificity. Sequence analysis of GH36, inspired by the observed structural differences, results in four distinct subgroups having clearly different active-site sequence motifs. This novel subdivision incorporates functional and architectural features and may aid further biochemical and structural analyses within GH36.
Crystal Structure of alpha-Galactosidase from Lactobacillus acidophilus NCFM: Insight into Tetramer Formation and Substrate Binding.,Fredslund F, Abou Hachem M, Jonsgaard Larsen R, Gerd Sorensen P, Coutinho PM, Lo Leggio L, Svensson B J Mol Biol. 2011 Jul 30. PMID:21827767[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Fredslund F, Abou Hachem M, Jonsgaard Larsen R, Gerd Sorensen P, Coutinho PM, Lo Leggio L, Svensson B. Crystal Structure of alpha-Galactosidase from Lactobacillus acidophilus NCFM: Insight into Tetramer Formation and Substrate Binding. J Mol Biol. 2011 Jul 30. PMID:21827767 doi:10.1016/j.jmb.2011.07.057
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