1i8t

==STRCUTURE OF UDP-GALACTOPYRANOSE MUTASE FROM E.COLI==

<table><tr><td colspan='2'>[[1i8t]] is a 2 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=1I8T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1I8T FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/UDP-galactopyranose_mutase UDP-galactopyranose mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.9 5.4.99.9] </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=1i8t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i8t OCA], [http://pdbe.org/1i8t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1i8t RCSB], [http://www.ebi.ac.uk/pdbsum/1i8t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1i8t ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/GLF_ECOLI GLF_ECOLI]] Catalyzes the interconversion through a 2-keto intermediate of uridine diphosphogalactopyranose (UDP-GalP) into uridine diphosphogalactofuranose (UDP-GalF) (By similarity).<ref>PMID:8576037</ref> <ref>PMID:11448178</ref>

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

Uridine diphosphogalactofuranose (UDP-Galf ) is the precursor of the d-galactofuranose (Galf ) residues found in bacterial and parasitic cell walls, including those of many pathogens, such as Mycobacterium tuberculosis and Trypanosoma cruzi. UDP-Galf is made from UDP-galactopyranose (UDP-Galp) by the enzyme UDP-galactopyranose mutase (mutase). The mutase enzyme is essential for the viability of mycobacteria and is not found in humans, making it a viable therapeutic target. The mechanism by which mutase achieves the unprecedented ring contraction of a nonreducing sugar is unclear. We have solved the crystal structure of Escherichia coli mutase to 2.4 A resolution. The novel structure shows that the flavin nucleotide is located in a cleft lined with conserved residues. Site-directed mutagenesis studies indicate that this cleft contains the active site, with the sugar ring of the substrate UDP-galactose adjacent to the exposed isoalloxazine ring of FAD. Assay results establish that the enzyme is active only when flavin is reduced. We conclude that mutase most likely functions by transient reduction of substrate.

UDP-galactopyranose mutase has a novel structure and mechanism.,Sanders DA, Staines AG, McMahon SA, McNeil MR, Whitfield C, Naismith JH Nat Struct Biol. 2001 Oct;8(10):858-63. PMID:11573090<ref>PMID:11573090</ref>

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

</div>

<div class="pdbe-citations 1i8t" style="background-color:#fffaf0;"></div>

*[[UDP-galactopyranose mutase|UDP-galactopyranose mutase]]

[[Category: Bacillus coli migula 1895]]

[[Category: McMahon, S A]]

[[Category: McNeil, M R]]

[[Category: Naismith, J H]]

[[Category: Sanders, D A.R]]

[[Category: Staines, A G]]

[[Category: Whitfield, C]]

[[Category: Udp-galactopyranose]]