1mac

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(New page: 200px<br /><applet load="1mac" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mac, resolution 2.3&Aring;" /> '''CRYSTAL STRUCTURE AND...)
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[[Image:1mac.jpg|left|200px]]<br /><applet load="1mac" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1mac, resolution 2.3&Aring;" />
 
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'''CRYSTAL STRUCTURE AND SITE-DIRECTED MUTAGENESIS OF BACILLUS MACERANS ENDO-1,3-1,4-BETA-GLUCANASE'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE AND SITE-DIRECTED MUTAGENESIS OF BACILLUS MACERANS ENDO-1,3-1,4-BETA-GLUCANASE==
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In beta-glucans those beta-1,4 glycosidic bonds which are adjacent to, beta-1,3 bonds are cleaved by endo-1,3-1,4-beta-glucanases, (beta-glucanases). Here, the relationship between structure and activity, of the beta-glucanase of Bacillus macerans is studied by x-ray, crystallography and site-directed mutagenesis of active site residues., Crystal structure analysis at 2.3-A resolution reveals a jelly-roll, protein structure with a deep active site channel harboring the amino acid, residues Trp101, Glu103, Asp105, and Glu107 as in the hybrid Bacillus, beta-glucanase H(A16-M) (Keitel, T., Simon, O., Borriss, R., and, Heinemann, U. (1993) Proc. Natl. Acad. Sci. U.S.A. 90, 5287-5291)., Different mutant proteins with substitutions in these residues are, generated by site-directed mutagenesis, isolated, and characterized., Compared with the wild-type enzyme their activity is reduced to less than, 1%. Several mutants with isosteric substitutions in Glu103 and Glu107 are, completely inactive, suggesting a direct role of these residues in, glycosyl bond hydrolysis. The kinetic properties of mutant beta-glucanases, and the crystal structure of the wild-type enzyme are consistent with a, mechanism where Glu103 and Glu107 are the catalytic amino acid residues, responsible for cleavage of the beta-1,4 glycosidic bond within the, substrate molecule.
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<StructureSection load='1mac' size='340' side='right'caption='[[1mac]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1mac]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Paenibacillus_macerans Paenibacillus macerans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MAC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MAC 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]] 2.3&#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=CA:CALCIUM+ION'>CA</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=1mac FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mac OCA], [https://pdbe.org/1mac PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mac RCSB], [https://www.ebi.ac.uk/pdbsum/1mac PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mac ProSAT]</span></td></tr>
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</table>
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== Function ==
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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/ma/1mac_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=1mac 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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In beta-glucans those beta-1,4 glycosidic bonds which are adjacent to beta-1,3 bonds are cleaved by endo-1,3-1,4-beta-glucanases (beta-glucanases). Here, the relationship between structure and activity of the beta-glucanase of Bacillus macerans is studied by x-ray crystallography and site-directed mutagenesis of active site residues. Crystal structure analysis at 2.3-A resolution reveals a jelly-roll protein structure with a deep active site channel harboring the amino acid residues Trp101, Glu103, Asp105, and Glu107 as in the hybrid Bacillus beta-glucanase H(A16-M) (Keitel, T., Simon, O., Borriss, R., and Heinemann, U. (1993) Proc. Natl. Acad. Sci. U.S.A. 90, 5287-5291). Different mutant proteins with substitutions in these residues are generated by site-directed mutagenesis, isolated, and characterized. Compared with the wild-type enzyme their activity is reduced to less than 1%. Several mutants with isosteric substitutions in Glu103 and Glu107 are completely inactive, suggesting a direct role of these residues in glycosyl bond hydrolysis. The kinetic properties of mutant beta-glucanases and the crystal structure of the wild-type enzyme are consistent with a mechanism where Glu103 and Glu107 are the catalytic amino acid residues responsible for cleavage of the beta-1,4 glycosidic bond within the substrate molecule.
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==About this Structure==
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Crystal structure and site-directed mutagenesis of Bacillus macerans endo-1,3-1,4-beta-glucanase.,Hahn M, Olsen O, Politz O, Borriss R, Heinemann U J Biol Chem. 1995 Feb 17;270(7):3081-8. PMID:7852389<ref>PMID:7852389</ref>
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1MAC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Paenibacillus_macerans Paenibacillus macerans] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MAC OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Crystal structure and site-directed mutagenesis of Bacillus macerans endo-1,3-1,4-beta-glucanase., Hahn M, Olsen O, Politz O, Borriss R, Heinemann U, J Biol Chem. 1995 Feb 17;270(7):3081-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7852389 7852389]
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</div>
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[[Category: Licheninase]]
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<div class="pdbe-citations 1mac" style="background-color:#fffaf0;"></div>
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[[Category: Paenibacillus macerans]]
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[[Category: Single protein]]
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[[Category: Hahn, M.]]
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[[Category: Heinemann, U.]]
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[[Category: CA]]
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[[Category: hydrolase (glucanase)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:16:26 2007''
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==See Also==
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*[[Glucanase 3D structures|Glucanase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Paenibacillus macerans]]
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[[Category: Hahn M]]
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[[Category: Heinemann U]]

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CRYSTAL STRUCTURE AND SITE-DIRECTED MUTAGENESIS OF BACILLUS MACERANS ENDO-1,3-1,4-BETA-GLUCANASE

PDB ID 1mac

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