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1rmg

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(New page: 200px<br /><applet load="1rmg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rmg, resolution 2.0&Aring;" /> '''RHAMNOGALACTURONASE A...)
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[[Image:1rmg.gif|left|200px]]<br /><applet load="1rmg" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1rmg, resolution 2.0&Aring;" />
 
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'''RHAMNOGALACTURONASE A FROM ASPERGILLUS ACULEATUS'''<br />
 
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==Overview==
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==RHAMNOGALACTURONASE A FROM ASPERGILLUS ACULEATUS==
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BACKGROUND: Pectic substances are the major polysaccharide components of, the middle lamella and primary cell wall of dicotyledonous plants. They, consist of homogalacturonan 'smooth' regions and highly rhamnified 'hairy', regions of rhamnogalacturonan. The backbone in rhamnogalacturonan-l, (RG-l), which is composed of alternating galacturonic acid and rhamnose, residues, is the substrate for a new class of enzymes known as, rhamnogalacturnoases (RGases). RGase A is a novel enzyme implicated in the, enzymatic degradation of RG-l. RESULTS: The structure of RGase A from, Aspergillus aculeatus has been solved by the single isomorphous, replacement method including anomalous scattering (SIRAS method) to 2.0 A, resolution. The enzyme folds into a large right-handed parallel beta, helix, with a core composed of 13 turns of beta strands. Four parallel, beta sheets (PB1, PB1a, PB2 and PB3), formed by the consecutive turns, are, typically separated by a residue in the conformation of a left-handed, alpha helix. As a consequence of the consecutive turns, 32% of all, residues have their sidechains aligned at the surface or in the interior, of the parallel beta helix. The aligned residues at the surface are, dominated by threonine, aspartic acid and asparagine, whereas valine, leucine and isoleucine are most frequently found in the interior. A very, large hydrophobic cavity is found in the interior of the parallel beta, helix. The potential active site is a groove, oriented almost, perpendicular to the helical axis, containing a cluster of three aspartic, acid residues and one glutamic acid residue. The enzyme is highly, glycosylated; two N-linked and eighteen O-linked glycosylation sites have, been found in the structure. CONCLUSIONS: Rhamnogalacturonase A from A., aculeatus is the first three-dimensional structure of an enzyme, hydrolyzing glycoside bonds within the backbone of RG-l. The large groove, which is the potential active site of RGase A, is also seen in the, structures of pectate lyases. Two catalytic aspartic acid residues, which, have been proposed to have a catalytic role, reside in this area of RGase, A. The distance between the aspartic acid residues is consistent with the, inverting mechanism of catalysis. The glycan groups bound to RGase A are, important to the stability of the crystal, as the carbohydrate moiety is, involved in most of the intermolecular hydrogen bonds.
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<StructureSection load='1rmg' size='340' side='right'caption='[[1rmg]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1rmg]] is a 1 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=1RMG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RMG FirstGlance]. <br>
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1RMG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_aculeatus Aspergillus aculeatus] with MAN, BMA and GLC as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RMG OCA].
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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&#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=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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==Reference==
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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=1rmg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rmg OCA], [https://pdbe.org/1rmg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rmg RCSB], [https://www.ebi.ac.uk/pdbsum/1rmg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rmg ProSAT]</span></td></tr>
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The crystal structure of rhamnogalacturonase A from Aspergillus aculeatus: a right-handed parallel beta helix., Petersen TN, Kauppinen S, Larsen S, Structure. 1997 Apr 15;5(4):533-44. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9115442 9115442]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RHGA_ASPAC RHGA_ASPAC] Pectinolytic enzymes consist of four classes of enzymes: pectine lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Has a positive effect in the apple hot-mash liquefaction process. Hydrolyzes alpha-D-galacturonopyranosyl-(1,2)-alpha-L-rhamnopyranosyl linkages in the backbone of the hairy regions of pectins.<ref>PMID:9464254</ref>
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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/rm/1rmg_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=1rmg ConSurf].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Aspergillus aculeatus]]
[[Category: Aspergillus aculeatus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Kauppinen, S.]]
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[[Category: Kauppinen S]]
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[[Category: Larsen, S.]]
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[[Category: Larsen S]]
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[[Category: Petersen, T.N.]]
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[[Category: Petersen TN]]
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[[Category: BMA]]
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[[Category: GLC]]
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[[Category: MAN]]
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[[Category: glycosidase]]
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[[Category: hydrolase]]
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[[Category: inverting]]
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[[Category: parallel beta-helix]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:42:37 2007''
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Current revision

RHAMNOGALACTURONASE A FROM ASPERGILLUS ACULEATUS

PDB ID 1rmg

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