1h4p

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[[Image:1h4p.gif|left|200px]]
 
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{{Structure
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==Crystal structure of exo-1,3-beta glucanse from Saccharomyces cerevisiae==
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|PDB= 1h4p |SIZE=350|CAPTION= <scene name='initialview01'>1h4p</scene>, resolution 1.75&Aring;
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<StructureSection load='1h4p' size='340' side='right'caption='[[1h4p]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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|SITE= <scene name='pdbsite=AC1:Nag+Binding+Site+For+Chain+B'>AC1</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene>
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<table><tr><td colspan='2'>[[1h4p]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H4P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H4P FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucan_1,3-beta-glucosidase Glucan 1,3-beta-glucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.58 3.2.1.58] </span>
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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]] 1.75&#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=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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|DOMAIN=
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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=1h4p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h4p OCA], [https://pdbe.org/1h4p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h4p RCSB], [https://www.ebi.ac.uk/pdbsum/1h4p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h4p ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h4p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h4p OCA], [http://www.ebi.ac.uk/pdbsum/1h4p PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1h4p RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/EXG1_YEAST EXG1_YEAST] Glucanases possibly play a role in cell expansion during growth, in cell-cell fusion during mating, and in spore release during sporulation. This enzyme hydrolyzes both 1,3-beta- and 1,6-beta-linkages and even has beta-glucosidase activity. It could also function biosynthetically as a transglycosylase.
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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/h4/1h4p_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=1h4p 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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We present in vitro data that explain the recognition mechanism of misfolded glycoproteins by UDP-glucose glycoprotein-glucosyltransferase (UGGT). The glycoprotein exo-(1,3)-beta-glucanase (beta-Glc) bearing two glycans unfolds in a pH-dependent manner to become a misfolded substrate for UGGT. In the crystal structure of this glycoprotein, the local hydrophobicity surrounding each glycosylation site coincides with the differential recognition of N-linked glycans by UGGT. We introduced a single F280S point mutation, producing a beta-Glc protein with full enzymatic activity that was both recognized as misfolded and monoglucosylated by UGGT. Contrary to current views, these data show that UGGT can modify N-linked glycans positioned at least 40 A from localized regions of disorder and sense subtle conformational changes within structurally compact, enzymatically active glycoprotein substrates.
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'''CRYSTAL STRUCTURE OF EXO-1,3-BETA GLUCANSE FROM SACCHAROMYCES CEREVISIAE'''
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The ER protein folding sensor UDP-glucose glycoprotein-glucosyltransferase modifies substrates distant to local changes in glycoprotein conformation.,Taylor SC, Ferguson AD, Bergeron JJ, Thomas DY Nat Struct Mol Biol. 2004 Feb;11(2):128-34. Epub 2004 Jan 4. PMID:14730348<ref>PMID:14730348</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1h4p" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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We present in vitro data that explain the recognition mechanism of misfolded glycoproteins by UDP-glucose glycoprotein-glucosyltransferase (UGGT). The glycoprotein exo-(1,3)-beta-glucanase (beta-Glc) bearing two glycans unfolds in a pH-dependent manner to become a misfolded substrate for UGGT. In the crystal structure of this glycoprotein, the local hydrophobicity surrounding each glycosylation site coincides with the differential recognition of N-linked glycans by UGGT. We introduced a single F280S point mutation, producing a beta-Glc protein with full enzymatic activity that was both recognized as misfolded and monoglucosylated by UGGT. Contrary to current views, these data show that UGGT can modify N-linked glycans positioned at least 40 A from localized regions of disorder and sense subtle conformational changes within structurally compact, enzymatically active glycoprotein substrates.
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*[[Beta-glucosidase 3D structures|Beta-glucosidase 3D structures]]
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*[[Glucanase 3D structures|Glucanase 3D structures]]
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==About this Structure==
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== References ==
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1H4P is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H4P OCA].
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<references/>
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__TOC__
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==Reference==
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</StructureSection>
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The ER protein folding sensor UDP-glucose glycoprotein-glucosyltransferase modifies substrates distant to local changes in glycoprotein conformation., Taylor SC, Ferguson AD, Bergeron JJ, Thomas DY, Nat Struct Mol Biol. 2004 Feb;11(2):128-34. Epub 2004 Jan 4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14730348 14730348]
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[[Category: Large Structures]]
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[[Category: Glucan 1,3-beta-glucosidase]]
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Single protein]]
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[[Category: Ferguson AD]]
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[[Category: Ferguson, A D.]]
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[[Category: glucan degradation]]
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[[Category: glycosidase]]
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[[Category: hydrolyase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:57:37 2008''
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Current revision

Crystal structure of exo-1,3-beta glucanse from Saccharomyces cerevisiae

PDB ID 1h4p

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