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1o7a

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[[Image:1o7a.gif|left|200px]]
 
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{{Structure
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==Human beta-Hexosaminidase B==
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|PDB= 1o7a |SIZE=350|CAPTION= <scene name='initialview01'>1o7a</scene>, resolution 2.25&Aring;
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<StructureSection load='1o7a' size='340' side='right'caption='[[1o7a]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
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|SITE= <scene name='pdbsite=ABC:N-Glycosylation+Site+3'>ABC</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=GDL:2-ACETAMIDO-2-DEOXY-D-GLUCONO-1,5-LACTONE'>GDL</scene> and <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>
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<table><tr><td colspan='2'>[[1o7a]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O7A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O7A FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Beta-N-acetylhexosaminidase Beta-N-acetylhexosaminidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.52 3.2.1.52]
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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]] 2.25&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GDL:2-ACETAMIDO-2-DEOXY-D-GLUCONO-1,5-LACTONE'>GDL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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}}
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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=1o7a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o7a OCA], [https://pdbe.org/1o7a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o7a RCSB], [https://www.ebi.ac.uk/pdbsum/1o7a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o7a ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/HEXB_HUMAN HEXB_HUMAN] Defects in HEXB are the cause of GM2-gangliosidosis type 2 (GM2G2) [MIM:[https://omim.org/entry/268800 268800]; also known as Sandhoff disease. GM2-gangliosidosis is an autosomal recessive lysosomal storage disease marked by the accumulation of GM2 gangliosides in the neuronal cells. GM2G2 is clinically indistinguishable from GM2-gangliosidosis type 1, presenting startle reactions, early blindness, progressive motor and mental deterioration, macrocephaly and cherry-red spots on the macula.<ref>PMID:1720305</ref> <ref>PMID:1531140</ref> <ref>PMID:8357844</ref> <ref>PMID:7626071</ref> <ref>PMID:7557963</ref> <ref>PMID:7633435</ref> <ref>PMID:8950198</ref> <ref>PMID:9401004</ref> <ref>PMID:9856491</ref> <ref>PMID:9694901</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/HEXB_HUMAN HEXB_HUMAN] Responsible for the degradation of GM2 gangliosides, and a variety of other molecules containing terminal N-acetyl hexosamines, in the brain and other tissues.
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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/o7/1o7a_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=1o7a ConSurf].
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<div style="clear:both"></div>
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'''HUMAN BETA-HEXOSAMINIDASE B'''
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==See Also==
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*[[Beta-Hexosaminidase|Beta-Hexosaminidase]]
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*[[Beta-Hexosaminidase 3D structures|Beta-Hexosaminidase 3D structures]]
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==Overview==
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*[[Beta-N-acetylhexosaminidase 3D structures|Beta-N-acetylhexosaminidase 3D structures]]
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Human lysosomal beta-hexosaminidases are dimeric enzymes composed of alpha and beta-chains, encoded by the genes HEXA and HEXB. They occur in three isoforms, the homodimeric hexosaminidases B (betabeta) and S (alphaalpha), and the heterodimeric hexosaminidase A (alphabeta), where dimerization is required for catalytic activity. Allelic variations in the HEXA and HEXB genes cause the fatal inborn errors of metabolism Tay-Sachs disease and Sandhoff disease, respectively. Here, we present the crystal structure of a complex of human beta-hexosaminidase B with a transition state analogue inhibitor at 2.3A resolution (pdb 1o7a). On the basis of this structure and previous studies on related enzymes, a retaining double-displacement mechanism for glycosyl hydrolysis by beta-hexosaminidase B is proposed. In the dimer structure, which is derived from an analysis of crystal packing, most of the mutations causing late-onset Sandhoff disease reside near the dimer interface and are proposed to interfere with correct dimer formation. The structure reported here is a valid template also for the dimeric structures of beta-hexosaminidase A and S.
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== References ==
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<references/>
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==Disease==
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__TOC__
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Known diseases associated with this structure: Sandhoff disease, infantile, juvenile, and adult forms OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=606873 606873]], Spinal muscular atrophy, juvenile OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=606873 606873]]
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</StructureSection>
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==About this Structure==
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1O7A is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O7A OCA].
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==Reference==
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The X-ray crystal structure of human beta-hexosaminidase B provides new insights into Sandhoff disease., Maier T, Strater N, Schuette CG, Klingenstein R, Sandhoff K, Saenger W, J Mol Biol. 2003 May 2;328(3):669-81. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12706724 12706724]
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[[Category: Beta-N-acetylhexosaminidase]]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Klingenstein, R.]]
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[[Category: Klingenstein R]]
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[[Category: Maier, T.]]
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[[Category: Maier T]]
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[[Category: Saenger, W.]]
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[[Category: Saenger W]]
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[[Category: Sandhoff, K.]]
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[[Category: Sandhoff K]]
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[[Category: Schuette, C.]]
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[[Category: Schuette C]]
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[[Category: Strater, N.]]
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[[Category: Strater N]]
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[[Category: EDO]]
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[[Category: GDL]]
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[[Category: NAG]]
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[[Category: ba8-barrel]]
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[[Category: glycosidase]]
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[[Category: glycosyl hydrolase]]
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[[Category: hexosaminidase]]
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[[Category: lysosomal]]
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[[Category: sandhoff disease]]
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[[Category: sphingolipid degradation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:06:43 2008''
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Current revision

Human beta-Hexosaminidase B

PDB ID 1o7a

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