1byh

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[[Image:1byh.gif|left|200px]]
 
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{{Structure
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==MOLECULAR AND ACTIVE-SITE STRUCTURE OF A BACILLUS (1-3,1-4)-BETA-GLUCANASE==
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|PDB= 1byh |SIZE=350|CAPTION= <scene name='initialview01'>1byh</scene>, resolution 2.8&Aring;
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<StructureSection load='1byh' size='340' side='right'caption='[[1byh]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GLC:GLUCOSE'>GLC</scene>, <scene name='pdbligand=NBU:N-BUTANE'>NBU</scene>
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<table><tr><td colspan='2'>[[1byh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BYH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BYH FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Licheninase Licheninase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.73 3.2.1.73] </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]] 2.8&#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=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NBU:N-BUTANE'>NBU</scene>, <scene name='pdbligand=PRD_900005:beta-cellobiose'>PRD_900005</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=1byh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1byh OCA], [https://pdbe.org/1byh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1byh RCSB], [https://www.ebi.ac.uk/pdbsum/1byh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1byh 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=1byh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1byh OCA], [http://www.ebi.ac.uk/pdbsum/1byh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1byh RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/GUB_PAEMA GUB_PAEMA]
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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/by/1byh_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1byh 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 three-dimensional structure of the hybrid Bacillus 1,3-1,4-beta-glucanase (beta-glucanase; 1,3-1,4-beta-D-glucan 4-glucanohydrolase, lichenase, EC 3.2.1.73) designated H(A16-M) was determined by x-ray crystallography at a resolution of 2.0 A and refined to an R value of 16.4% using stereochemical restraints. The protein molecule consists mainly of two seven-stranded antiparallel beta-pleated sheets arranged atop each other to form a compact, sandwich-like structure. A channel crossing one side of the protein molecule accommodates an inhibitor, 3,4-epoxybutyl beta-D-cellobioside, which binds covalently to the side chain of Glu-105, as seen in a crystal structure analysis at 2.8-A resolution of the protein-inhibitor complex (R = 16.8%). That Glu-105 may be indispensible for enzyme catalysis by H(A16-M) is suggested by site-directed mutagenesis of this residue, which inevitably leads to an inactive enzyme.
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'''MOLECULAR AND ACTIVE-SITE STRUCTURE OF A BACILLUS (1-3,1-4)-BETA-GLUCANASE'''
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Molecular and active-site structure of a Bacillus 1,3-1,4-beta-glucanase.,Keitel T, Simon O, Borriss R, Heinemann U Proc Natl Acad Sci U S A. 1993 Jun 1;90(11):5287-91. PMID:8099449<ref>PMID:8099449</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 1byh" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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The three-dimensional structure of the hybrid Bacillus 1,3-1,4-beta-glucanase (beta-glucanase; 1,3-1,4-beta-D-glucan 4-glucanohydrolase, lichenase, EC 3.2.1.73) designated H(A16-M) was determined by x-ray crystallography at a resolution of 2.0 A and refined to an R value of 16.4% using stereochemical restraints. The protein molecule consists mainly of two seven-stranded antiparallel beta-pleated sheets arranged atop each other to form a compact, sandwich-like structure. A channel crossing one side of the protein molecule accommodates an inhibitor, 3,4-epoxybutyl beta-D-cellobioside, which binds covalently to the side chain of Glu-105, as seen in a crystal structure analysis at 2.8-A resolution of the protein-inhibitor complex (R = 16.8%). That Glu-105 may be indispensible for enzyme catalysis by H(A16-M) is suggested by site-directed mutagenesis of this residue, which inevitably leads to an inactive enzyme.
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*[[Glucanase 3D structures|Glucanase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1BYH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BYH OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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Molecular and active-site structure of a Bacillus 1,3-1,4-beta-glucanase., Keitel T, Simon O, Borriss R, Heinemann U, Proc Natl Acad Sci U S A. 1993 Jun 1;90(11):5287-91. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8099449 8099449]
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[[Category: Licheninase]]
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[[Category: Single protein]]
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[[Category: Synthetic construct]]
[[Category: Synthetic construct]]
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[[Category: Heinemann, U.]]
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[[Category: Heinemann U]]
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[[Category: Keitel, T.]]
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[[Category: Keitel T]]
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[[Category: hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:10:54 2008''
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Current revision

MOLECULAR AND ACTIVE-SITE STRUCTURE OF A BACILLUS (1-3,1-4)-BETA-GLUCANASE

PDB ID 1byh

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