2g3m: Difference between revisions
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==Crystal structure of the Sulfolobus solfataricus alpha-glucosidase MalA== | ==Crystal structure of the Sulfolobus solfataricus alpha-glucosidase MalA== | ||
<StructureSection load='2g3m' size='340' side='right' caption='[[2g3m]], [[Resolution|resolution]] 2.55Å' scene=''> | <StructureSection load='2g3m' size='340' side='right'caption='[[2g3m]], [[Resolution|resolution]] 2.55Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2g3m]] is a 6 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2g3m]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/'saccharolobus_solfataricus' 'saccharolobus solfataricus']. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G3M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2G3M FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2g3n|2g3n]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2g3n|2g3n]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">malA ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">malA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2287 'Saccharolobus solfataricus'])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Alpha-glucosidase Alpha-glucosidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.20 3.2.1.20] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2g3m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g3m OCA], [https://pdbe.org/2g3m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2g3m RCSB], [https://www.ebi.ac.uk/pdbsum/2g3m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2g3m ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/AGLU_SULSO AGLU_SULSO]] Major soluble alpha-glucosidase (By similarity). | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
*[[Alpha-glucosidase|Alpha-glucosidase]] | *[[Alpha-glucosidase 3D structures|Alpha-glucosidase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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[[Category: Saccharolobus solfataricus]] | [[Category: Saccharolobus solfataricus]] | ||
[[Category: Alpha-glucosidase]] | [[Category: Alpha-glucosidase]] | ||
[[Category: Large Structures]] | |||
[[Category: Blum, P]] | [[Category: Blum, P]] | ||
[[Category: Ernst, H A]] | [[Category: Ernst, H A]] | ||
Revision as of 21:45, 10 March 2021
Crystal structure of the Sulfolobus solfataricus alpha-glucosidase MalACrystal structure of the Sulfolobus solfataricus alpha-glucosidase MalA
Structural highlights
Function[AGLU_SULSO] Major soluble alpha-glucosidase (By similarity). 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 alpha-glucosidase MalA from Sulfolobus solfataricus has been determined at 2.5Angstrom resolution. It provides a structural model for enzymes representing the major specificity in glycoside hydrolase family 31 (GH31), including alpha-glucosidases from higher organisms, involved in glycogen degradation and glycoprotein processing. The structure of MalA shows clear differences from the only other structure known from GH31, alpha-xylosidase YicI. MalA and YicI share only 23% sequence identity. Although the two enzymes display a similar domain structure and both form hexamers, their structures differ significantly in quaternary organization: MalA is a dimer of trimers, YicI a trimer of dimers. MalA and YicI also differ in their substrate specificities, as shown by kinetic measurements on model chromogenic substrates. In addition, MalA has a clear preference for maltose (Glc-alpha1,4-Glc), whereas YicI prefers isoprimeverose (Xyl-alpha1,6-Glc). The structural origin of this difference occurs in the -1 subsite where MalA residues Asp251 and Trp284 could interact with OH6 of the substrate. The structure of MalA in complex with beta-octyl-glucopyranoside has been determined. It reveals Arg400, Asp87, Trp284, Met321 and Phe327 as invariant residues forming the +1 subsite in the GH31 alpha-glucosidases. Structural comparisons with other GH families suggest that the GH31 enzymes belong to clan GH-D. Structure of the Sulfolobus solfataricus alpha-glucosidase: implications for domain conservation and substrate recognition in GH31.,Ernst HA, Lo Leggio L, Willemoes M, Leonard G, Blum P, Larsen S J Mol Biol. 2006 May 12;358(4):1106-24. Epub 2006 Mar 13. PMID:16580018[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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