2g3m: Difference between revisions
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[[Image:2g3m.gif|left|200px]] | [[Image:2g3m.gif|left|200px]] | ||
'''Crystal structure of the Sulfolobus solfataricus alpha-glucosidase MalA''' | {{Structure | ||
|PDB= 2g3m |SIZE=350|CAPTION= <scene name='initialview01'>2g3m</scene>, resolution 2.55Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Alpha-glucosidase Alpha-glucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.20 3.2.1.20] | |||
|GENE= malA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2287 Sulfolobus solfataricus]) | |||
}} | |||
'''Crystal structure of the Sulfolobus solfataricus alpha-glucosidase MalA''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2G3M is a [ | 2G3M is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G3M OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16580018 16580018] | ||
[[Category: Alpha-glucosidase]] | [[Category: Alpha-glucosidase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: retaining mechanism]] | [[Category: retaining mechanism]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:00:00 2008'' | ||
Revision as of 18:00, 20 March 2008
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| , resolution 2.55Å | |||||||
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| Gene: | malA (Sulfolobus solfataricus) | ||||||
| Activity: | Alpha-glucosidase, with EC number 3.2.1.20 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the Sulfolobus solfataricus alpha-glucosidase MalA
OverviewOverview
The 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.
About this StructureAbout this Structure
2G3M is a Single protein structure of sequence from Sulfolobus solfataricus. Full crystallographic information is available from OCA.
ReferenceReference
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
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