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2ou4

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Revision as of 17:56, 10 September 2015

Crystal structure of D-tagatose 3-epimerase from Pseudomonas cichorii

Structural highlights

2ou4 is a 4 chain structure with sequence from "bacterium_cichorii"_(swingle_1925)_elliott_1930 "bacterium cichorii" (swingle 1925) elliott 1930. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

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

Pseudomonas cichoriiid-tagatose 3-epimerase (P. cichoriid-TE) can efficiently catalyze the epimerization of not only d-tagatose to d-sorbose, but also d-fructose to d-psicose, and is used for the production of d-psicose from d-fructose. The crystal structures of P. cichoriid-TE alone and in complexes with d-tagatose and d-fructose were determined at resolutions of 1.79, 2.28, and 2.06 A, respectively. A subunit of P. cichoriid-TE adopts a (beta/alpha)(8) barrel structure, and a metal ion (Mn(2+)) found in the active site is coordinated by Glu152, Asp185, His211, and Glu246 at the end of the beta-barrel. P. cichoriid-TE forms a stable dimer to give a favorable accessible surface for substrate binding on the front side of the dimer. The simulated omit map indicates that O2 and O3 of d-tagatose and/or d-fructose coordinate Mn(2+), and that C3-O3 is located between carboxyl groups of Glu152 and Glu246, supporting the previously proposed mechanism of deprotonation/protonation at C3 by two Glu residues. Although the electron density is poor at the 4-, 5-, and 6-positions of the substrates, substrate-enzyme interactions can be deduced from the significant electron density at O6. The O6 possibly interacts with Cys66 via hydrogen bonding, whereas O4 and O5 in d-tagatose and O4 in d-fructose do not undergo hydrogen bonding to the enzyme and are in a hydrophobic environment created by Phe7, Trp15, Trp113, and Phe248. Due to the lack of specific interactions between the enzyme and its substrates at the 4- and 5-positions, P. cichoriid-TE loosely recognizes substrates in this region, allowing it to efficiently catalyze the epimerization of d-tagatose and d-fructose (C4 epimer of d-tagatose) as well. Furthermore, a C3-O3 proton-exchange mechanism for P. cichoriid-TE is suggested by X-ray structural analysis, providing a clear explanation for the regulation of the ionization state of Glu152 and Glu246.

Crystal structures of D-tagatose 3-epimerase from Pseudomonas cichorii and its complexes with D-tagatose and D-fructose.,Yoshida H, Yamada M, Nishitani T, Takada G, Izumori K, Kamitori S J Mol Biol. 2007 Nov 23;374(2):443-53. Epub 2007 Sep 19. PMID:17936787^[1]

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

References

↑ Yoshida H, Yamada M, Nishitani T, Takada G, Izumori K, Kamitori S. Crystal structures of D-tagatose 3-epimerase from Pseudomonas cichorii and its complexes with D-tagatose and D-fructose. J Mol Biol. 2007 Nov 23;374(2):443-53. Epub 2007 Sep 19. PMID:17936787 doi:http://dx.doi.org/10.1016/j.jmb.2007.09.033

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2ou4"

@@ Line 2: / Line 2: @@
 <StructureSection load='2ou4' size='340' side='right' caption='[[2ou4]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2ou4]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_cichorii Pseudomonas cichorii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OU4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2OU4 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2ou4]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacterium_cichorii"_(swingle_1925)_elliott_1930 "bacterium cichorii" (swingle 1925) elliott 1930]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OU4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2OU4 FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></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=2ou4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ou4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ou4 RCSB], [http://www.ebi.ac.uk/pdbsum/2ou4 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=2ou4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ou4 OCA], [http://pdbe.org/2ou4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ou4 RCSB], [http://www.ebi.ac.uk/pdbsum/2ou4 PDBsum]</span></td></tr>
 </table>
 == Evolutionary Conservation ==
@@ Line 24: / Line 24: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2ou4" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Pseudomonas cichorii]]
 [[Category: Izumori, K]]
 [[Category: Kamitori, S]]

2ou4

From Proteopedia

Revision as of 17:56, 10 September 2015

Crystal structure of D-tagatose 3-epimerase from Pseudomonas cichorii

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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