1obb

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(New page: 200px<br /> <applet load="1obb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1obb, resolution 1.90&Aring;" /> '''ALPHA-GLUCOSIDASE A...)
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[[Image:1obb.gif|left|200px]]<br />
 
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<applet load="1obb" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1obb, resolution 1.90&Aring;" />
 
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'''ALPHA-GLUCOSIDASE A, AGLA, FROM THERMOTOGA MARITIMA IN COMPLEX WITH MALTOSE AND NAD+'''<br />
 
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==Overview==
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==alpha-glucosidase A, AglA, from Thermotoga maritima in complex with maltose and NAD+==
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Glycoside hydrolase family 4 represents an unusual group of glucosidases, with a requirement for NAD+, divalent metal cations, and reducing, conditions. The family is also unique in its inclusion of both alpha- and, beta-specific enzymes. The alpha-glucosidase A, AglA, from Thermotoga, maritima is a typical glycoside hydrolase family 4 enzyme, requiring NAD+, and Mn2+ as well as strongly reducing conditions for activity. Here we, present the crystal structure of the protein complexed with NAD+ and, maltose, refined at a resolution of 1.9 A. The NAD+ is bound to a typical, Rossman fold NAD+-binding site, and the nicotinamide moiety is localized, close to the maltose substrate. Within the active site the conserved, Cys-174 and surrounding histidines are positioned to play a role in the, ... [[http://ispc.weizmann.ac.il/pmbin/getpm?12588867 (full description)]]
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<StructureSection load='1obb' size='340' side='right'caption='[[1obb]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1obb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OBB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OBB FirstGlance]. <br>
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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]] 1.9&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</scene></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=1obb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1obb OCA], [https://pdbe.org/1obb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1obb RCSB], [https://www.ebi.ac.uk/pdbsum/1obb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1obb ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AGLA_THEMA AGLA_THEMA] alpha-glycosidase with a very broad specificity hydrolyzes maltose and other small maltooligosaccharides but is inactive against the polymeric substrate starch agla is not specific with respect to the configuration at the c-4 position of its substrates because glycosidic derivatives of d-galactose are also hydrolyzed does not cleave beta-glycosidic bonds
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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/ob/1obb_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=1obb ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1OBB is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]] with MAL and NAD as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OBB OCA]].
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*[[Alpha-glucosidase 3D structures|Alpha-glucosidase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structure of Thermotoga maritima alpha-glucosidase AglA defines a new clan of NAD+-dependent glycosidases., Lodge JA, Maier T, Liebl W, Hoffmann V, Strater N, J Biol Chem. 2003 May 23;278(21):19151-8. Epub 2003 Feb 14. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12588867 12588867]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Thermotoga maritima MSB8]]
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[[Category: Thermotoga maritima]]
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[[Category: Hoffmann V]]
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[[Category: Hoffmann, V.]]
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[[Category: Liebl W]]
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[[Category: Liebl, W.]]
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[[Category: Lodge JA]]
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[[Category: Lodge, J.A.]]
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[[Category: Maier T]]
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[[Category: Maier, T.]]
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[[Category: Strater N]]
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[[Category: Strater, N.]]
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[[Category: MAL]]
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[[Category: NAD]]
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[[Category: glycosidase]]
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[[Category: hydrolase]]
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[[Category: maltose]]
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[[Category: nad+]]
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[[Category: sulfinic acid]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 17:29:54 2007''
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Current revision

alpha-glucosidase A, AglA, from Thermotoga maritima in complex with maltose and NAD+

PDB ID 1obb

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