This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1dex

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1dex" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dex, resolution 1.90&Aring;" /> '''RHAMNOGALACTURONAN A...)
Current revision (09:50, 20 March 2024) (edit) (undo)
 
(16 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1dex.jpg|left|200px]]<br /><applet load="1dex" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1dex, resolution 1.90&Aring;" />
 
-
'''RHAMNOGALACTURONAN ACETYLESTERASE FROM ASPERGILLUS ACULEATUS AT 1.9 A RESOLUTION'''<br />
 
-
==Overview==
+
==RHAMNOGALACTURONAN ACETYLESTERASE FROM ASPERGILLUS ACULEATUS AT 1.9 A RESOLUTION==
-
BACKGROUND: The complex polysaccharide rhamnogalacturonan constitutes a, major part of the hairy region of pectin. It can have different types of, carbohydrate sidechains attached to the rhamnose residues in the backbone, of alternating rhamnose and galacturonic acid residues; the galacturonic, acid residues can be methylated or acetylated. Aspergillus aculeatus, produces enzymes that are able to perform a synergistic degradation of, rhamnogalacturonan. The deacetylation of the backbone by, rhamnogalacturonan acetylesterase (RGAE) is an essential prerequisite for, the subsequent action of the enzymes that cleave the glycosidic bonds., RESULTS: The structure of RGAE has been determined at 1.55 A resolution., RGAE folds into an alpha/beta/alpha structure. The active site of RGAE is, an open cleft containing a serine-histidine-aspartic acid catalytic triad., The position of the three residues relative to the central parallel beta, sheet and the lack of the nucleophilic elbow motif found in structures, possessing the alpha/beta hydrolase fold show that RGAE does not belong to, the alpha/beta hydrolase family. CONCLUSIONS: Structural and sequence, comparisons have revealed that, despite very low sequence similarities, RGAE is related to seven other proteins. They are all members of a new, hydrolase family, the SGNH-hydrolase family, which includes the, carbohydrate esterase family 12 as a distinct subfamily. The, SGNH-hydrolase family is characterised by having four conserved blocks of, residues, each with one completely conserved residue; serine, glycine, asparagine and histidine, respectively. Each of the four residues plays a, role in the catalytic function.
+
<StructureSection load='1dex' size='340' side='right'caption='[[1dex]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
-
 
+
== Structural highlights ==
-
==About this Structure==
+
<table><tr><td colspan='2'>[[1dex]] 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=1DEX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DEX FirstGlance]. <br>
-
1DEX 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 NAG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DEX OCA].
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
-
 
+
<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=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-
==Reference==
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dex FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dex OCA], [https://pdbe.org/1dex PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dex RCSB], [https://www.ebi.ac.uk/pdbsum/1dex PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dex ProSAT]</span></td></tr>
-
Rhamnogalacturonan acetylesterase elucidates the structure and function of a new family of hydrolases., Molgaard A, Kauppinen S, Larsen S, Structure. 2000 Apr 15;8(4):373-83. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10801485 10801485]
+
</table>
 +
== Function ==
 +
[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 ==
 +
[[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/de/1dex_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=1dex ConSurf].
 +
<div style="clear:both"></div>
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
[[Category: Aspergillus aculeatus]]
[[Category: Aspergillus aculeatus]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Kauppinen, S.]]
+
[[Category: Kauppinen S]]
-
[[Category: Larsen, S.]]
+
[[Category: Larsen S]]
-
[[Category: Molgaard, A.]]
+
[[Category: Molgaard A]]
-
[[Category: NAG]]
+
-
[[Category: sgnh hydrolase]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:13:47 2007''
+

Current revision

RHAMNOGALACTURONAN ACETYLESTERASE FROM ASPERGILLUS ACULEATUS AT 1.9 A RESOLUTION

PDB ID 1dex

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1dex"
Personal tools