2xn0: Difference between revisions
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The | ==Structure of alpha-galactosidase from Lactobacillus acidophilus NCFM, PtCl4 derivative== | ||
<StructureSection load='2xn0' size='340' side='right'caption='[[2xn0]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2xn0]] is a 2 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=2XN0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XN0 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]] 2.5Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PT:PLATINUM+(II)+ION'>PT</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=2xn0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xn0 OCA], [https://pdbe.org/2xn0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xn0 RCSB], [https://www.ebi.ac.uk/pdbsum/2xn0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xn0 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/MELA_LACAC MELA_LACAC] Hydrolyzes the short-chain alpha-galactosaccharide raffinose. | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:21827767</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2xn0" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Galactosidase 3D structures|Galactosidase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Lactobacillus acidophilus NCFM]] | |||
[[Category: Large Structures]] | |||
[[Category: Abou Hachem M]] | |||
[[Category: Fredslund F]] | |||
[[Category: Larsen RJ]] | |||
[[Category: Lo Leggio L]] | |||
[[Category: Sorensen PG]] | |||
[[Category: Svensson B]] | |||
Latest revision as of 16:58, 1 February 2024
Structure of alpha-galactosidase from Lactobacillus acidophilus NCFM, PtCl4 derivativeStructure of alpha-galactosidase from Lactobacillus acidophilus NCFM, PtCl4 derivative
Structural highlights
FunctionMELA_LACAC Hydrolyzes the short-chain alpha-galactosaccharide raffinose. Publication Abstract from PubMedLactobacillus 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 AlsoReferences
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