1i8t
From Proteopedia
(New page: 200px<br /><applet load="1i8t" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i8t, resolution 2.4Å" /> '''STRCUTURE OF UDP-GALA...) |
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| - | [[Image:1i8t.jpg|left|200px]]<br /><applet load="1i8t" size=" | + | [[Image:1i8t.jpg|left|200px]]<br /><applet load="1i8t" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1i8t, resolution 2.4Å" /> | caption="1i8t, resolution 2.4Å" /> | ||
'''STRCUTURE OF UDP-GALACTOPYRANOSE MUTASE FROM E.COLI'''<br /> | '''STRCUTURE OF UDP-GALACTOPYRANOSE MUTASE FROM E.COLI'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Uridine diphosphogalactofuranose (UDP-Galf ) is the precursor of the | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1I8T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with FAD as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http:// | + | 1I8T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=FAD:'>FAD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I8T OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: UDP-galactopyranose mutase]] | [[Category: UDP-galactopyranose mutase]] | ||
| - | [[Category: McMahon, S | + | [[Category: McMahon, S A.]] |
| - | [[Category: McNeil, M | + | [[Category: McNeil, M R.]] |
| - | [[Category: Naismith, J | + | [[Category: Naismith, J H.]] |
| - | [[Category: Sanders, D | + | [[Category: Sanders, D A.R.]] |
| - | [[Category: Staines, A | + | [[Category: Staines, A G.]] |
[[Category: Whitfield, C.]] | [[Category: Whitfield, C.]] | ||
[[Category: FAD]] | [[Category: FAD]] | ||
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[[Category: udp-galactopyranose]] | [[Category: udp-galactopyranose]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:09:12 2008'' |
Revision as of 11:09, 21 February 2008
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STRCUTURE OF UDP-GALACTOPYRANOSE MUTASE FROM E.COLI
Overview
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.
About this Structure
1I8T is a Single protein structure of sequence from Escherichia coli with as ligand. Active as UDP-galactopyranose mutase, with EC number 5.4.99.9 Full crystallographic information is available from OCA.
Reference
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
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