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1hjq

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[[Image:1hjq.gif|left|200px]]<br />
 
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<applet load="1hjq" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1hjq, resolution 2.55&Aring;" />
 
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'''STRUCTURE OF TWO FUNGAL BETA-1,4-GALACTANASES: SEARCHING FOR THE BASIS FOR TEMPERATURE AND PH OPTIMUM.'''<br />
 
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==Overview==
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==Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum.==
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beta-1,4-Galactanases hydrolyze the galactan side chains that are part of, the complex carbohydrate structure of the pectin. They are assigned to, family 53 of the glycoside hydrolases and display significant variations, in their pH and temperature optimum and stability. Two fungal, beta-1,4-galactanases from Myceliophthora thermophila and Humicola, insolens have been cloned and heterologously expressed, and the crystal, structures of the gene products were determined. The structures are, compared to the previously only known family 53 structure of the, galactanase from Aspergillus aculeatus (AAGAL) showing approximately 56%, identity. The M. thermophila and H. insolens galactanases are thermophilic, enzymes and are most active at neutral to basic pH, whereas AAGAL is, mesophilic and most active at acidic pH. The structure of the M., thermophila galactanase (MTGAL) was determined from crystals obtained with, HEPES and TRIS buffers to 1.88 A and 2.14 A resolution, respectively. The, structure of the H. insolens galactanase (HIGAL) was determined to 2.55 A, resolution. The thermostability of MTGAL and HIGAL correlates with, increase in the protein rigidity and electrostatic interactions, stabilization of the alpha-helices, and a tighter packing. An inspection, of the active sites in the three enzymes identifies several amino acid, substitutions that could explain the variation in pH optimum. Examination, of the activity as a function of pH for the D182N mutant of AAGAL and the, A90S/ H91D mutant of MTGAL showed that the difference in pH optimum, between AAGAL and MTGAL is at least partially associated with differences, in the nature of residues at positions 182, 90, and/or 91.
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<StructureSection load='1hjq' size='340' side='right'caption='[[1hjq]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1hjq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Humicola_insolens Humicola insolens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HJQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HJQ 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]] 2.55&#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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=1hjq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hjq OCA], [https://pdbe.org/1hjq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hjq RCSB], [https://www.ebi.ac.uk/pdbsum/1hjq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hjq ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GANA_HUMIN GANA_HUMIN]
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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/hj/1hjq_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=1hjq 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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1HJQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Humicola_insolens Humicola insolens] with NAG as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Arabinogalactan_endo-1,4-beta-galactosidase Arabinogalactan endo-1,4-beta-galactosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.89 3.2.1.89] Structure known Active Site: NAG. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HJQ OCA].
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*[[Beta-1%2C4-galactanase|Beta-1%2C4-galactanase]]
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__TOC__
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==Reference==
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</StructureSection>
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Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum., Le Nours J, Ryttersgaard C, Lo Leggio L, Ostergaard PR, Borchert TV, Christensen LL, Larsen S, Protein Sci. 2003 Jun;12(6):1195-204. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12761390 12761390]
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[[Category: Arabinogalactan endo-1,4-beta-galactosidase]]
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[[Category: Humicola insolens]]
[[Category: Humicola insolens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Borchert, T.V.]]
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[[Category: Borchert TV]]
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[[Category: Christensen, L.L.H.]]
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[[Category: Christensen LLH]]
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[[Category: Larsen, S.]]
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[[Category: Larsen S]]
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[[Category: Leggio, L.Lo.]]
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[[Category: Le Nours J]]
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[[Category: Nours, J.Le.]]
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[[Category: Lo Leggio L]]
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[[Category: Ostergaard, P.R.]]
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[[Category: Ostergaard PR]]
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[[Category: Ryttersgaard, C.]]
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[[Category: Ryttersgaard C]]
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[[Category: NAG]]
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[[Category: 4-galactanases]]
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[[Category: alkalophile]]
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[[Category: beta-1]]
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[[Category: clan gh-a]]
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[[Category: family 53 glycoside hydrolase]]
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[[Category: ph optimum]]
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[[Category: thermophile]]
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[[Category: thermostability]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 16:37:15 2007''
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Current revision

Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum.

PDB ID 1hjq

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