2h1f: Difference between revisions
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'''E. coli heptosyltransferase WaaC with ADP''' | {{Structure | ||
|PDB= 2h1f |SIZE=350|CAPTION= <scene name='initialview01'>2h1f</scene>, resolution 2.400Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene> | |||
|ACTIVITY= | |||
|GENE= rfaC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=217992 Escherichia coli O6]) | |||
}} | |||
'''E. coli heptosyltransferase WaaC with ADP''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2H1F is a [ | 2H1F is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_o6 Escherichia coli o6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H1F OCA]. | ||
==Reference== | ==Reference== | ||
Structure of the Escherichia coli heptosyltransferase WaaC: binary complexes with ADP and ADP-2-deoxy-2-fluoro heptose., Grizot S, Salem M, Vongsouthi V, Durand L, Moreau F, Dohi H, Vincent S, Escaich S, Ducruix A, J Mol Biol. 2006 Oct 20;363(2):383-94. Epub 2006 Jul 29. PMID:[http:// | Structure of the Escherichia coli heptosyltransferase WaaC: binary complexes with ADP and ADP-2-deoxy-2-fluoro heptose., Grizot S, Salem M, Vongsouthi V, Durand L, Moreau F, Dohi H, Vincent S, Escaich S, Ducruix A, J Mol Biol. 2006 Oct 20;363(2):383-94. Epub 2006 Jul 29. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16963083 16963083] | ||
[[Category: Escherichia coli o6]] | [[Category: Escherichia coli o6]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: gt-b fold absence of c-terminal alpha-helix]] | [[Category: gt-b fold absence of c-terminal alpha-helix]] | ||
''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 17:11:28 2008'' | ||
Revision as of 15:11, 20 March 2008
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| 2h1f, resolution 2.400Å | |||||||||||||
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| Ligands: | ADP | ||||||||||||
| Gene: | rfaC (Escherichia coli O6) | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
E. coli heptosyltransferase WaaC with ADP
Overview
Lipopolysaccharides constitute the outer leaflet of the outer membrane of Gram-negative bacteria and are therefore essential for cell growth and viability. The heptosyltransferase WaaC is a glycosyltransferase (GT) involved in the synthesis of the inner core region of LPS. It catalyzes the addition of the first L-glycero-D-manno-heptose (heptose) molecule to one 3-deoxy-D-manno-oct-2-ulosonic acid (Kdo) residue of the Kdo2-lipid A molecule. Heptose is an essential component of the LPS core domain; its absence results in a truncated lipopolysaccharide associated with the deep-rough phenotype causing a greater susceptibility to antibiotic and an attenuated virulence for pathogenic Gram-negative bacteria. Thus, WaaC represents a promising target in antibacterial drug design. Here, we report the structure of WaaC from the Escherichia coli pathogenic strain RS218 alone at 1.9 A resolution, and in complex with either ADP or the non-cleavable analog ADP-2-deoxy-2-fluoro-heptose of the sugar donor at 2.4 A resolution. WaaC adopts the GT-B fold in two domains, characteristic of one glycosyltransferase structural superfamily. The comparison of the three different structures shows that WaaC does not undergo a domain rotation, characteristic of the GT-B family, upon substrate binding, but allows the substrate analog and the reaction product to adopt remarkably distinct conformations inside the active site. In addition, both binary complexes offer a close view of the donor subsite and, together with results from site-directed mutagenesis studies, provide evidence for a model of the catalytic mechanism.
About this Structure
2H1F is a Single protein structure of sequence from Escherichia coli o6. Full crystallographic information is available from OCA.
Reference
Structure of the Escherichia coli heptosyltransferase WaaC: binary complexes with ADP and ADP-2-deoxy-2-fluoro heptose., Grizot S, Salem M, Vongsouthi V, Durand L, Moreau F, Dohi H, Vincent S, Escaich S, Ducruix A, J Mol Biol. 2006 Oct 20;363(2):383-94. Epub 2006 Jul 29. PMID:16963083
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