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2h1h

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[[Image:2h1h.jpg|left|200px]]<br /><applet load="2h1h" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2h1h.jpg|left|200px]]
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caption="2h1h, resolution 2.400&Aring;" />
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'''E. coli heptosyltransferase WaaC with ADP-2-deoxy-2-fluoro heptose'''<br />
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{{Structure
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|PDB= 2h1h |SIZE=350|CAPTION= <scene name='initialview01'>2h1h</scene>, resolution 2.400&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=AFH:ADENOSINE-5'-DIPHOSPHATE-2-DEOXY-2-FLUORO HEPTOSE'>AFH</scene>
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|ACTIVITY=
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|GENE= rfaC, rfa-2, waaC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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}}
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'''E. coli heptosyltransferase WaaC with ADP-2-deoxy-2-fluoro heptose'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2H1H 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=AFH:'>AFH</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H1H OCA].
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2H1H is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H1H OCA].
==Reference==
==Reference==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=16963083 16963083]
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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]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: gt-b fold]]
[[Category: gt-b fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:37:14 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:11:31 2008''

Revision as of 15:11, 20 March 2008


PDB ID 2h1h

Drag the structure with the mouse to rotate
, resolution 2.400Å
Ligands:
Gene: rfaC, rfa-2, waaC (Escherichia coli)
Coordinates: save as pdb, mmCIF, xml



E. coli heptosyltransferase WaaC with ADP-2-deoxy-2-fluoro heptose


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

2H1H is a Single protein structure of sequence from Escherichia coli. 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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