2bi8: Difference between revisions
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[[Image:2bi8.jpg|left|200px]]<br /><applet load="2bi8" size=" | [[Image:2bi8.jpg|left|200px]]<br /><applet load="2bi8" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2bi8, resolution 2.35Å" /> | caption="2bi8, resolution 2.35Å" /> | ||
'''UDP-GALACTOPYRANOSE MUTASE FROM KLEBSIELLA PNEUMONIAE WITH REDUCED FAD'''<br /> | '''UDP-GALACTOPYRANOSE MUTASE FROM KLEBSIELLA PNEUMONIAE WITH REDUCED FAD'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
2BI8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Klebsiella_pneumoniae Klebsiella pneumoniae] 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] Known structural/functional Site: <scene name='pdbsite=AC1:Fad Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http:// | 2BI8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Klebsiella_pneumoniae Klebsiella pneumoniae] 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] Known structural/functional Site: <scene name='pdbsite=AC1:Fad+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BI8 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: lipopolysaccharide biosynthesis]] | [[Category: lipopolysaccharide biosynthesis]] | ||
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Revision as of 11:24, 3 February 2008
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UDP-GALACTOPYRANOSE MUTASE FROM KLEBSIELLA PNEUMONIAE WITH REDUCED FAD
OverviewOverview
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 StructureAbout this Structure
2BI8 is a Single protein structure of sequence from Klebsiella pneumoniae with as ligand. Active as UDP-galactopyranose mutase, with EC number 5.4.99.9 Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
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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