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1hjq

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Revision as of 09:23, 10 January 2018

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

Structural highlights

1hjq is a 1 chain structure with sequence from Atcc 16454. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1hjs, 1hju
Activity:	Arabinogalactan endo-beta-1,4-galactanase, with EC number 3.2.1.89
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Evolutionary Conservation

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

Publication Abstract from PubMed

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.

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:12761390^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Le Nours J, Ryttersgaard C, Lo Leggio L, Ostergaard PR, Borchert TV, Christensen LL, Larsen S. Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. Protein Sci. 2003 Jun;12(6):1195-204. PMID:12761390

1 Structural highlights
2 Evolutionary Conservation
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1hjq"

@@ Line 1: / Line 1: @@
-==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.==
 <StructureSection load='1hjq' size='340' side='right' caption='[[1hjq]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
 == Structural highlights ==
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1hjs|1hjs]], [[1hju|1hju]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Arabinogalactan_endo-beta-1,4-galactanase Arabinogalactan endo-beta-1,4-galactanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.89 3.2.1.89] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hjq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hjq OCA], [http://pdbe.org/1hjq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hjq RCSB], [http://www.ebi.ac.uk/pdbsum/1hjq PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hjq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hjq OCA], [http://pdbe.org/1hjq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hjq RCSB], [http://www.ebi.ac.uk/pdbsum/1hjq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1hjq ProSAT]</span></td></tr>
 </table>
 == Evolutionary Conservation ==
@@ Line 12: / Line 13: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hj/1hjq_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hj/1hjq_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 27: / Line 28: @@
 </div>
 <div class="pdbe-citations 1hjq" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Beta-1%2C4-galactanase|Beta-1%2C4-galactanase]]
 == References ==
 <references/>

1hjq

From Proteopedia

Revision as of 09:23, 10 January 2018

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

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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