1pp4

From Proteopedia

(Difference between revisions)

Revision as of 13:01, 12 October 2017

The crystal structure of rhamnogalacturonan acetylesterase in space group P3121

Structural highlights

1pp4 is a 2 chain structure with sequence from Aspac. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1deo, 1dex, 1k7c
Gene:	RHA1 (ASPAC)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1pp4"

Categories: Aspac | Larsen, S | Molgaard, A | Hydrolase

@@ Line 1: / Line 1: @@
 ==The crystal structure of rhamnogalacturonan acetylesterase in space group P3121==
 <StructureSection load='1pp4' size='340' side='right' caption='[[1pp4]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1deo|1deo]], [[1dex|1dex]], [[1k7c|1k7c]]</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'>[http://oca.weizmann.ac.il/oca-docs/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]</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=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>
 == Function ==

1pp4

From Proteopedia

Revision as of 13:01, 12 October 2017

The crystal structure of rhamnogalacturonan acetylesterase in space group P3121

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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