1x8d

<table><tr><td colspan='2'>[[1x8d]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X8D OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1X8D FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=RNS:L-RHAMNOSE'>RNS</scene></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1x8d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x8d OCA], [http://pdbe.org/1x8d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1x8d RCSB], [http://www.ebi.ac.uk/pdbsum/1x8d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1x8d ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/RHAM_ECOLI RHAM_ECOLI]] Involved in the anomeric conversion of L-rhamnose.<ref>PMID:15060078</ref>

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== Publication Abstract from PubMed ==

The crystal structure of Escherichia coli rhamnose mutarotase (YiiL) is completely different from the previously reported structures of the Lactococcus lactis galactose mutarotase and the Bacillus subtilis RbsD (pyranase). YiiL exists as a locally asymmetric dimer, which is stabilized by an intermolecular beta-sheet, various hydrophobic interactions, and a cation-pi interaction with a salt-bridge. The protein folds of YiiL are similar to those of a Streptomyces coelicolor mono-oxygenase and a hypothetical Arabidopsis thaliana protein At3g17210. By assaying the enzymatic activity of six active-site mutants and by comparing the crystal structure-derived active site conformations of YiiL, RbsD, and a galactose mutarotase, we were able to define the amino acid residues required for catalysis and suggest a possible catalytic mechanism for YiiL. Although the active-site amino acid residues of YiiL (His, Tyr, and Trp) differ greatly from those of galactose mutarotase (His, Glu, and Asp), their geometries, which determine the structures of the preferred monosaccharide substrates, are conserved. In addition, the in vivo function of YiiL was assessed by constructing a mutant E.coli strain that carries a yiiL deletion. The presence of the yiiL gene is critical for efficient cell growth only when concentrations of l-rhamnose are limited.

Structural insights into the monosaccharide specificity of Escherichia coli rhamnose mutarotase.,Ryu KS, Kim JI, Cho SJ, Park D, Park C, Cheong HK, Lee JO, Choi BS J Mol Biol. 2005 May 27;349(1):153-62. Epub 2005 Apr 7. PMID:15876375<ref>PMID:15876375</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 1x8d" style="background-color:#fffaf0;"></div>

[[Category: Bacillus coli migula 1895]]

[[Category: Cho, S J]]

[[Category: Choi, B S]]

[[Category: Kim, J I]]

[[Category: Lee, J O]]

[[Category: Park, C]]

[[Category: Park, D]]

[[Category: Ryu, K S]]

[[Category: Mutarotase]]