2g3m

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[[Image:2g3m.gif|left|200px]]
 
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==Crystal structure of the Sulfolobus solfataricus alpha-glucosidase MalA==
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The line below this paragraph, containing "STRUCTURE_2g3m", creates the "Structure Box" on the page.
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<StructureSection load='2g3m' size='340' side='right'caption='[[2g3m]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.55&#8491;</td></tr>
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<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>
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{{STRUCTURE_2g3m| PDB=2g3m | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AGLU_SACS2 AGLU_SACS2] Major soluble alpha-glucosidase.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g3/2g3m_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2g3m ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''Crystal structure of the Sulfolobus solfataricus alpha-glucosidase MalA'''
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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<ref>PMID:16580018</ref>
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==Overview==
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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.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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].
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</div>
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<div class="pdbe-citations 2g3m" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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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]
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*[[Alpha-glucosidase 3D structures|Alpha-glucosidase 3D structures]]
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[[Category: Alpha-glucosidase]]
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== References ==
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[[Category: Single protein]]
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<references/>
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[[Category: Sulfolobus solfataricus]]
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__TOC__
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[[Category: Blum, P.]]
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</StructureSection>
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[[Category: Ernst, H A.]]
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[[Category: Large Structures]]
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[[Category: Larsen, S.]]
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[[Category: Saccharolobus solfataricus]]
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[[Category: Leggio, L Lo.]]
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[[Category: Blum P]]
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[[Category: Leonard, G.]]
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[[Category: Ernst HA]]
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[[Category: Willemoes, M.]]
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[[Category: Larsen S]]
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[[Category: Alpha-glucosidase]]
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[[Category: Leonard G]]
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[[Category: Glycoside hydrolase family 31]]
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[[Category: Lo Leggio L]]
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[[Category: Hydrolase]]
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[[Category: Willemoes M]]
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[[Category: Multidomain protein]]
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[[Category: Retaining mechanism]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:39:02 2008''
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Current revision

Crystal structure of the Sulfolobus solfataricus alpha-glucosidase MalA

PDB ID 2g3m

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