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1i8t

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Revision as of 03:01, 11 September 2015

STRCUTURE OF UDP-GALACTOPYRANOSE MUTASE FROM E.COLI

Structural highlights

1i8t is a 2 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Activity:	UDP-galactopyranose mutase, with EC number 5.4.99.9
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[GLF_ECOLI] Catalyzes the interconversion through a 2-keto intermediate of uridine diphosphogalactopyranose (UDP-GalP) into uridine diphosphogalactofuranose (UDP-GalF) (By similarity).^[1] ^[2]

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

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^[3]

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

References

↑ Nassau PM, Martin SL, Brown RE, Weston A, Monsey D, McNeil MR, Duncan K. Galactofuranose biosynthesis in Escherichia coli K-12: identification and cloning of UDP-galactopyranose mutase. J Bacteriol. 1996 Feb;178(4):1047-52. PMID:8576037
↑ Zhang Q, Liu H. Mechanistic investigation of UDP-galactopyranose mutase from Escherichia coli using 2- and 3-fluorinated UDP-galactofuranose as probes. J Am Chem Soc. 2001 Jul 18;123(28):6756-66. PMID:11448178
↑ Sanders DA, Staines AG, McMahon SA, McNeil MR, Whitfield C, Naismith JH. UDP-galactopyranose mutase has a novel structure and mechanism. Nat Struct Biol. 2001 Oct;8(10):858-63. PMID:11573090 doi:http://dx.doi.org/10.1038/nsb1001-858

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1i8t"

@@ Line 5: / Line 5: @@
 </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://www.rcsb.org/pdb/explore.do?structureId=1i8t RCSB], [http://www.ebi.ac.uk/pdbsum/1i8t 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=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]</span></td></tr>
 </table>
 == Function ==
@@ Line 27: / Line 27: @@
 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>
 ==See Also==

1i8t

From Proteopedia

Revision as of 03:01, 11 September 2015

STRCUTURE OF UDP-GALACTOPYRANOSE MUTASE FROM E.COLI

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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