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2pyh

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Revision as of 08:47, 29 August 2018

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

Structural highlights

2pyh is a 2 chain structure with sequence from Azotobacter vinelandii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	2pyg
Gene:	algE4 (Azotobacter vinelandii)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Alginate is a family of linear copolymers of (1-->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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Rozeboom HJ, Bjerkan TM, Kalk KH, Ertesvag H, Holtan S, Aachmann FL, Valla S, Dijkstra BW. Structural and mutational characterization of the catalytic A-module of the mannuronan C-5-epimerase AlgE4 from Azotobacter vinelandii. J Biol Chem. 2008 Aug 29;283(35):23819-28. Epub 2008 Jun 23. PMID:18574239 doi:10.1074/jbc.M804119200

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/2pyh"

@@ Line 1: / Line 1: @@
 ==Azotobacter vinelandii Mannuronan C-5 epimerase AlgE4 A-module complexed with mannuronan trisaccharide==
 <StructureSection load='2pyh' size='340' side='right' caption='[[2pyh]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2pyg|2pyg]]</td></tr>
 <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>
-<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://pdbe.org/2pyh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2pyh RCSB], [http://www.ebi.ac.uk/pdbsum/2pyh 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=2pyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pyh OCA], [http://pdbe.org/2pyh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2pyh RCSB], [http://www.ebi.ac.uk/pdbsum/2pyh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2pyh ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/py/2pyh_consurf.spt"</scriptWhenChecked>
+    <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>
     <text>to colour the structure by Evolutionary Conservation</text>

2pyh

From Proteopedia

Revision as of 08:47, 29 August 2018

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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