2g3m: Difference between revisions

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-[[Image:2g3m.gif|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_2g3m", creates the "Structure Box" on the page.
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-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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-{{STRUCTURE_2g3m|  PDB=2g3m  |  SCENE=  }}
-'''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]] 2.55&Aring;' scene=''>
+== Structural highlights ==
+<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='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>
+<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>
+== Function ==
+[https://www.uniprot.org/uniprot/AGLU_SACS2 AGLU_SACS2] Major soluble alpha-glucosidase.
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g3/2g3m_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-==Overview==
+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>
-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 Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-G3M 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].
+</div>
+<div class="pdbe-citations 2g3m" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-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]
+*[[Alpha-glucosidase 3D structures|Alpha-glucosidase 3D structures]]
-[[Category: Alpha-glucosidase]]
+== References ==
-[[Category: Single protein]]
+<references/>
-[[Category: Sulfolobus solfataricus]]
+__TOC__
-[[Category: Blum, P.]]
+</StructureSection>
-[[Category: Ernst, H A.]]
+[[Category: Large Structures]]
-[[Category: Larsen, S.]]
+[[Category: Saccharolobus solfataricus]]
-[[Category: Leggio, L Lo.]]
+[[Category: Blum P]]
-[[Category: Leonard, G.]]
+[[Category: Ernst HA]]
-[[Category: Willemoes, M.]]
+[[Category: Larsen S]]
-[[Category: Alpha-glucosidase]]
+[[Category: Leonard G]]
-[[Category: Glycoside hydrolase family 31]]
+[[Category: Lo Leggio L]]
-[[Category: Hydrolase]]
+[[Category: Willemoes M]]
-[[Category: Multidomain protein]]
-[[Category: Retaining mechanism]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 04:39:02 2008''