1wam
From Proteopedia
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| - | [[Image:1wam.gif|left|200px]] | + | [[Image:1wam.gif|left|200px]] |
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| - | '''STRUCTURE OF UDP-GALACTOPYRANOSE MUTASE FROM KLEBSIELLA PNEUMONIAE WITH FADH-''' | + | {{Structure |
| + | |PDB= 1wam |SIZE=350|CAPTION= <scene name='initialview01'>1wam</scene>, resolution 2.35Å | ||
| + | |SITE= <scene name='pdbsite=AC1:Fad+Binding+Site+For+Chain+A'>AC1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE DINUCLEOTIDE'>FAD</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''STRUCTURE OF UDP-GALACTOPYRANOSE MUTASE FROM KLEBSIELLA PNEUMONIAE WITH FADH-''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1WAM is a [ | + | 1WAM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Klebsiella_pneumoniae Klebsiella pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WAM OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structures of Mycobacteria tuberculosis and Klebsiella pneumoniae UDP-galactopyranose mutase in the oxidised state and Klebsiella pneumoniae UDP-galactopyranose mutase in the (active) reduced state., Beis K, Srikannathasan V, Liu H, Fullerton SW, Bamford VA, Sanders DA, Whitfield C, McNeil MR, Naismith JH, J Mol Biol. 2005 May 13;348(4):971-82. PMID:[http:// | + | Crystal structures of Mycobacteria tuberculosis and Klebsiella pneumoniae UDP-galactopyranose mutase in the oxidised state and Klebsiella pneumoniae UDP-galactopyranose mutase in the (active) reduced state., Beis K, Srikannathasan V, Liu H, Fullerton SW, Bamford VA, Sanders DA, Whitfield C, McNeil MR, Naismith JH, J Mol Biol. 2005 May 13;348(4):971-82. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15843027 15843027] |
[[Category: Klebsiella pneumoniae]] | [[Category: Klebsiella pneumoniae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: lipopolysaccharide biosynthesis]] | [[Category: lipopolysaccharide biosynthesis]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:54:26 2008'' |
Revision as of 12:54, 20 March 2008
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| , resolution 2.35Å | |||||||
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| Sites: | |||||||
| Ligands: | |||||||
| Activity: | UDP-galactopyranose mutase, with EC number 5.4.99.9 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF UDP-GALACTOPYRANOSE MUTASE FROM KLEBSIELLA PNEUMONIAE WITH FADH-
Overview
Uridine diphosphogalactofuranose (UDP-Galf) is the precursor of the d-galactofuranose sugar found in bacterial and parasitic cell walls, including those of many pathogens. UDP-Galf is made from UDP-galactopyranose by the enzyme UDP-galactopyranose mutase. The enzyme requires the reduced FADH- co-factor for activity. The structure of the Mycobacterium tuberculosis mutase with FAD has been determined to 2.25 A. The structures of Klebsiella pneumoniae mutase with FAD and with FADH- bound have been determined to 2.2 A and 2.35 A resolution, respectively. This is the first report of the FADH(-)-containing structure. Two flavin-dependent mechanisms for the enzyme have been proposed, one, which involves a covalent adduct being formed at the flavin and the other based on electron transfer. Using our structural data, we have examined the two mechanisms. The electron transfer mechanism is consistent with the structural data, not surprisingly, since it makes fewer demands on the precise positioning of atoms. A model based on a covalent adduct FAD requires repositioning of the enzyme active site and would appear to require the isoalloxazine ring of FADH- to buckle in a particular way. However, the FADH- structure reveals that the isoalloxazine ring buckles in the opposite sense, this apparently requires the covalent adduct to trigger profound conformational changes in the protein or to buckle the FADH- opposite to that seen in the apo structure.
About this Structure
1WAM is a Single protein structure of sequence from Klebsiella pneumoniae. Full crystallographic information is available from OCA.
Reference
Crystal structures of Mycobacteria tuberculosis and Klebsiella pneumoniae UDP-galactopyranose mutase in the oxidised state and Klebsiella pneumoniae UDP-galactopyranose mutase in the (active) reduced state., Beis K, Srikannathasan V, Liu H, Fullerton SW, Bamford VA, Sanders DA, Whitfield C, McNeil MR, Naismith JH, J Mol Biol. 2005 May 13;348(4):971-82. PMID:15843027
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