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2pyh

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==Azotobacter vinelandii Mannuronan C-5 epimerase AlgE4 A-module complexed with mannuronan trisaccharide==
==Azotobacter vinelandii Mannuronan C-5 epimerase AlgE4 A-module complexed with mannuronan trisaccharide==
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<StructureSection load='2pyh' size='340' side='right' caption='[[2pyh]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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<StructureSection load='2pyh' size='340' side='right'caption='[[2pyh]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2pyh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PYH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PYH FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2pyh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PYH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PYH FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MAV:ALPHA-D-MANNOPYRANURONIC+ACID'>MAV</scene></td></tr>
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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]] 2.7&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2pyg|2pyg]]</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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MAV:ALPHA-D-MANNOPYRANURONIC+ACID'>MAV</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">algE4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=354 Azotobacter vinelandii])</td></tr>
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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=2pyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pyh OCA], [https://pdbe.org/2pyh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pyh RCSB], [https://www.ebi.ac.uk/pdbsum/2pyh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pyh ProSAT]</span></td></tr>
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<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=2pyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pyh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2pyh RCSB], [http://www.ebi.ac.uk/pdbsum/2pyh PDBsum]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/ALGE4_AZOVI ALGE4_AZOVI]] Converts beta-D-mannuronic acid (M) to alpha-L-guluronic acid (G), but introduces almost exclusively MG blocks, producing a polymer with non-gel-forming capacity.
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[https://www.uniprot.org/uniprot/ALGE4_AZOVI ALGE4_AZOVI] Converts beta-D-mannuronic acid (M) to alpha-L-guluronic acid (G), but introduces almost exclusively MG blocks, producing a polymer with non-gel-forming capacity.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/py/2pyh_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/py/2pyh_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</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/chain_selection.php?pdb_ID=2ata ConSurf].
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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=2pyh ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Alginate is a family of linear copolymers of (1--&gt;4)-linked beta-d-mannuronic acid and its C-5 epimer alpha-l-guluronic acid. The polymer is first produced as polymannuronic acid and the guluronic acid residues are then introduced at the polymer level by mannuronan C-5-epimerases. The structure of the catalytic A-module of the Azotobacter vinelandii mannuronan C-5-epimerase AlgE4 has been determined by x-ray crystallography at 2.1-A resolution. AlgE4A folds into a right-handed parallel beta-helix structure originally found in pectate lyase C and subsequently in several polysaccharide lyases and hydrolases. The beta-helix is composed of four parallel beta-sheets, comprising 12 complete turns, and has an amphipathic alpha-helix near the N terminus. The catalytic site is positioned in a positively charged cleft formed by loops extending from the surface encompassing Asp(152), an amino acid previously shown to be important for the reaction. Site-directed mutagenesis further implicates Tyr(149), His(154), and Asp(178) as being essential for activity. Tyr(149) probably acts as the proton acceptor, whereas His(154) is the proton donor in the epimerization reaction.
 
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Structural and mutational characterization of the catalytic A-module of the mannuronan C-5-epimerase AlgE4 from Azotobacter vinelandii.,Rozeboom HJ, Bjerkan TM, Kalk KH, Ertesvag H, Holtan S, Aachmann FL, Valla S, Dijkstra BW J Biol Chem. 2008 Aug 29;283(35):23819-28. Epub 2008 Jun 23. PMID:18574239<ref>PMID:18574239</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Azotobacter vinelandii]]
[[Category: Azotobacter vinelandii]]
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[[Category: Aachman, F L]]
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[[Category: Large Structures]]
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[[Category: Bjerkan, T M]]
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[[Category: Aachman FL]]
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[[Category: Dijkstra, B W]]
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[[Category: Bjerkan TM]]
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[[Category: Ertesvag, H]]
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[[Category: Dijkstra BW]]
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[[Category: Holtan, S]]
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[[Category: Ertesvag H]]
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[[Category: Kalk, K H]]
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[[Category: Holtan S]]
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[[Category: Rozeboom, H J]]
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[[Category: Kalk KH]]
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[[Category: Valla, S]]
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[[Category: Rozeboom HJ]]
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[[Category: Beta-helix]]
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[[Category: Valla S]]
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[[Category: Epimerase]]
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[[Category: Isomerase]]
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[[Category: Mannuronic acid]]
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Current revision

Azotobacter vinelandii Mannuronan C-5 epimerase AlgE4 A-module complexed with mannuronan trisaccharide

PDB ID 2pyh

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