2g3n: Difference between revisions

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[[Image:2g3n.gif|left|200px]]<br /><applet load="2g3n" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:2g3n.gif|left|200px]]
caption="2g3n, resolution 2.55&Aring;" />
 
'''Crystal structure of the Sulfolobus solfataricus alpha-glucosidase MalA in complex with beta-octyl-glucopyranoside'''<br />
{{Structure
|PDB= 2g3n |SIZE=350|CAPTION= <scene name='initialview01'>2g3n</scene>, resolution 2.55&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>
|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 in complex with beta-octyl-glucopyranoside'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
2G3N is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus] with <scene name='pdbligand=BOG:'>BOG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G3N OCA].  
2G3N 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=2G3N 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://ispc.weizmann.ac.il//pmbin/getpm?pmid=16580018 16580018]
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]]


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Revision as of 17:59, 20 March 2008

File:2g3n.gif


PDB ID 2g3n

Drag the structure with the mouse to rotate
, resolution 2.55Å
Ligands:
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 in complex with beta-octyl-glucopyranoside


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

2G3N 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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