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[[Image:1hju.gif|left|200px]]<br />
<applet load="1hju" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1hju, resolution 2.15&Aring;" />
'''STRUCTURE OF TWO FUNGAL BETA-1,4-GALACTANASES: SEARCHING FOR THE BASIS FOR TEMPERATURE AND PH OPTIMUM.'''<br />


==Overview==
==Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum.==
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.
<StructureSection load='1hju' size='340' side='right'caption='[[1hju]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1hju]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermothelomyces_thermophilus Thermothelomyces thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HJU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HJU FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15&#8491;</td></tr>
<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>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hju FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hju OCA], [https://pdbe.org/1hju PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hju RCSB], [https://www.ebi.ac.uk/pdbsum/1hju PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hju ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GANA_THETO GANA_THETO]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hj/1hju_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1hju ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1HJU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Corynascus_heterothallicus Corynascus heterothallicus] with NAG, SO4, TRS and PEG as [http://en.wikipedia.org/wiki/ligands ligands]. 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: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HJU OCA].
*[[Beta-1%2C4-galactanase|Beta-1%2C4-galactanase]]
 
__TOC__
==Reference==
</StructureSection>
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]
[[Category: Large Structures]]
[[Category: Arabinogalactan endo-1,4-beta-galactosidase]]
[[Category: Thermothelomyces thermophilus]]
[[Category: Corynascus heterothallicus]]
[[Category: Borchert TV]]
[[Category: Single protein]]
[[Category: Christensen LLH]]
[[Category: Borchert, T.V.]]
[[Category: Larsen S]]
[[Category: Christensen, L.L.H.]]
[[Category: Le Nours J]]
[[Category: Larsen, S.]]
[[Category: Lo Leggio L]]
[[Category: Leggio, L.Lo.]]
[[Category: Ostergaard PR]]
[[Category: Nours, J.Le.]]
[[Category: Ryttersgaard C]]
[[Category: Ostergaard, P.R.]]
[[Category: Ryttersgaard, C.]]
[[Category: NAG]]
[[Category: PEG]]
[[Category: SO4]]
[[Category: TRS]]
[[Category: 4-galactanases]]
[[Category: alkalophile]]
[[Category: beta-1]]
[[Category: clan gh-a]]
[[Category: family 53 glycoside hydrolase]]
[[Category: hydrolase]]
[[Category: ph optimum]]
[[Category: thermophile]]
[[Category: thermostability]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov  5 16:37:19 2007''

Latest revision as of 14:32, 27 March 2024

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

Structural highlights

1hju is a 4 chain structure with sequence from Thermothelomyces thermophilus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.15Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GANA_THETO

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1hju, resolution 2.15Å

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OCA
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