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| | <StructureSection load='1pp4' size='340' side='right'caption='[[1pp4]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='1pp4' size='340' side='right'caption='[[1pp4]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1pp4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspac Aspac]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PP4 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1PP4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1pp4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_aculeatus Aspergillus aculeatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PP4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PP4 FirstGlance]. <br> |
| - | </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></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1deo|1deo]], [[1dex|1dex]], [[1k7c|1k7c]]</div></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></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RHA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5053 ASPAC])</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=1pp4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pp4 OCA], [https://pdbe.org/1pp4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pp4 RCSB], [https://www.ebi.ac.uk/pdbsum/1pp4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pp4 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1pp4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pp4 OCA], [http://pdbe.org/1pp4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pp4 RCSB], [http://www.ebi.ac.uk/pdbsum/1pp4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1pp4 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RHA1_ASPAC RHA1_ASPAC]] Plays a key role in the degradation of rhamnogalacturonan in the cell wall. Acts in synergy together with rhamnogalacturonase A (RGase A) and rhamnogalacturonase B (RGase B).<ref>PMID:7592973</ref> | + | [https://www.uniprot.org/uniprot/RHA1_ASPAC RHA1_ASPAC] Plays a key role in the degradation of rhamnogalacturonan in the cell wall. Acts in synergy together with rhamnogalacturonase A (RGase A) and rhamnogalacturonase B (RGase B).<ref>PMID:7592973</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aspac]] | + | [[Category: Aspergillus aculeatus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Larsen, S]] | + | [[Category: Larsen S]] |
| - | [[Category: Molgaard, A]] | + | [[Category: Molgaard A]] |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
RHA1_ASPAC Plays a key role in the degradation of rhamnogalacturonan in the cell wall. Acts in synergy together with rhamnogalacturonase A (RGase A) and rhamnogalacturonase B (RGase B).[1]
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
The glycoprotein rhamnogalacturonan acetylesterase from Aspergillus aculeatus has been crystallized in two crystal forms, an orthorhombic and a trigonal crystal form. In the orthorhombic crystal form, the covalently bound carbohydrate at one of the two N-glycosylation sites is involved in crystal contacts. The orthorhombic crystal form was obtained at pH 5.0 and the trigonal crystal form at pH 4.5. In one case, the two crystal forms were found in the same drop at pH 4.7. The differences in crystal packing in the two crystal forms can be explained by the pH-dependent variation in the protonation state of the glutamic acid residues on the protein surface.
Crystal packing in two pH-dependent crystal forms of rhamnogalacturonan acetylesterase.,Molgaard A, Larsen S Acta Crystallogr D Biol Crystallogr. 2004 Mar;60(Pt 3):472-8. Epub 2004, Feb 25. PMID:14993671[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kauppinen S, Christgau S, Kofod LV, Halkier T, Dorreich K, Dalboge H. Molecular cloning and characterization of a rhamnogalacturonan acetylesterase from Aspergillus aculeatus. Synergism between rhamnogalacturonan degrading enzymes. J Biol Chem. 1995 Nov 10;270(45):27172-8. PMID:7592973
- ↑ Molgaard A, Larsen S. Crystal packing in two pH-dependent crystal forms of rhamnogalacturonan acetylesterase. Acta Crystallogr D Biol Crystallogr. 2004 Mar;60(Pt 3):472-8. Epub 2004, Feb 25. PMID:14993671 doi:10.1107/S0907444903029767
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