3ww4

<StructureSection load='3ww4' size='340' side='right'caption='[[3ww4]], [[Resolution|resolution]] 1.95&Aring;' scene=''>

<table><tr><td colspan='2'>[[3ww4]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WW4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WW4 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3BU:L-ALLOSE'>3BU</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=WOO:BETA-L-ALLOPYRANOSE'>WOO</scene></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ww4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ww4 OCA], [https://pdbe.org/3ww4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ww4 RCSB], [https://www.ebi.ac.uk/pdbsum/3ww4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ww4 ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

L-Ribose isomerase from Cellulomonas parahominis MB426 (CpL-RI) can catalyze the isomerization between L-ribose and L-ribulose, which are non-abundant in nature and called rare sugars. CpL-RI has a broad substrate specificity and can catalyze the isomerization between D-lyxose and D-xylulose, D-talose and D-tagatose, L-allose and L-psicose, L-gulose and L-sorbose, and D-mannose and D-fructose. To elucidate the molecular basis underlying the substrate recognition mechanism of CpL-RI, the crystal structures of CpL-RI alone and in complexes with L-ribose, L-allose, and L-psicose were determined. The structure of CpL-RI was very similar to that of L-ribose isomerase from Acinetobacter sp. strain DL-28, previously determined by us. CpL-RI had a cupin-type beta-barrel structure, and the catalytic site was detected between two large beta-sheets with a bound metal ion. The bound substrates coordinated to the metal ion, and Glu113 and Glu204 were shown to act as acid/base catalysts in the catalytic reaction via a cis-enediol intermediate. Glu211 and Arg243 were found to be responsible for the recognition of substrates with various configurations at 4- and 5-positions of sugar. CpL-RI formed a homo-tetramer in crystals, and the catalytic site independently consisted of residues within a subunit, suggesting that the catalytic site acted independently. Crystal structure and site-direct mutagenesis analyses showed that the tetramer structure is essential for the enzyme activity and that each subunit of CpL-RI could be structurally stabilized by intermolecular contacts with other subunits. The results of growth complementation assays suggest that CpL-RI is involved in a novel metabolic pathway using L-ribose as a carbon source.

Essentiality of tetramer formation of Cellulomonas parahominis L-ribose isomerase involved in novel L-ribose metabolic pathway.,Terami Y, Yoshida H, Uechi K, Morimoto K, Takata G, Kamitori S Appl Microbiol Biotechnol. 2015 Feb 8. PMID:25661811<ref>PMID:25661811</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 3ww4" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Kamitori, S]]

[[Category: Takata, G]]

[[Category: Terami, Y]]

[[Category: Yoshida, H]]

[[Category: Isomerase]]