1ro7
From Proteopedia
(New page: 200px<br /><applet load="1ro7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ro7, resolution 1.80Å" /> '''Structural analysis ...) |
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| - | [[Image:1ro7.gif|left|200px]]<br /><applet load="1ro7" size=" | + | [[Image:1ro7.gif|left|200px]]<br /><applet load="1ro7" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ro7, resolution 1.80Å" /> | caption="1ro7, resolution 1.80Å" /> | ||
'''Structural analysis of the sialyltransferase CstII from Campylobacter jejuni in complex with a substrate analogue, CMP-3FNeuAc.'''<br /> | '''Structural analysis of the sialyltransferase CstII from Campylobacter jejuni in complex with a substrate analogue, CMP-3FNeuAc.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Sialic acid terminates oligosaccharide chains on mammalian and microbial | + | Sialic acid terminates oligosaccharide chains on mammalian and microbial cell surfaces, playing critical roles in recognition and adherence. The enzymes that transfer the sialic acid moiety from cytidine-5'-monophospho-N-acetyl-neuraminic acid (CMP-NeuAc) to the terminal positions of these key glycoconjugates are known as sialyltransferases. Despite their important biological roles, little is understood about the mechanism or molecular structure of these membrane-associated enzymes. We report the first structure of a sialyltransferase, that of CstII from Campylobacter jejuni, a highly prevalent foodborne pathogen. Our structural, mutagenesis and kinetic data provide support for a novel mode of substrate binding and glycosyl transfer mechanism, including essential roles of a histidine (general base) and two tyrosine residues (coordination of the phosphate leaving group). This work provides a framework for understanding the activity of several sialyltransferases, from bacterial to human, and for the structure-based design of specific inhibitors. |
==About this Structure== | ==About this Structure== | ||
| - | 1RO7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Campylobacter_jejuni Campylobacter jejuni] with CSF and MPD as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1RO7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Campylobacter_jejuni Campylobacter jejuni] with <scene name='pdbligand=CSF:'>CSF</scene> and <scene name='pdbligand=MPD:'>MPD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RO7 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Campylobacter jejuni]] | [[Category: Campylobacter jejuni]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Chiu, C | + | [[Category: Chiu, C P.]] |
[[Category: Gilbert, M.]] | [[Category: Gilbert, M.]] | ||
| - | [[Category: Lairson, L | + | [[Category: Lairson, L L.]] |
[[Category: Lim, D.]] | [[Category: Lim, D.]] | ||
| - | [[Category: Strynadka, N | + | [[Category: Strynadka, N C.]] |
| - | [[Category: Wakarchuk, W | + | [[Category: Wakarchuk, W W.]] |
| - | [[Category: Watts, A | + | [[Category: Watts, A G.]] |
| - | [[Category: Withers, S | + | [[Category: Withers, S G.]] |
[[Category: CSF]] | [[Category: CSF]] | ||
[[Category: MPD]] | [[Category: MPD]] | ||
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[[Category: rossmann fold]] | [[Category: rossmann fold]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:52:52 2008'' |
Revision as of 12:52, 21 February 2008
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Structural analysis of the sialyltransferase CstII from Campylobacter jejuni in complex with a substrate analogue, CMP-3FNeuAc.
Overview
Sialic acid terminates oligosaccharide chains on mammalian and microbial cell surfaces, playing critical roles in recognition and adherence. The enzymes that transfer the sialic acid moiety from cytidine-5'-monophospho-N-acetyl-neuraminic acid (CMP-NeuAc) to the terminal positions of these key glycoconjugates are known as sialyltransferases. Despite their important biological roles, little is understood about the mechanism or molecular structure of these membrane-associated enzymes. We report the first structure of a sialyltransferase, that of CstII from Campylobacter jejuni, a highly prevalent foodborne pathogen. Our structural, mutagenesis and kinetic data provide support for a novel mode of substrate binding and glycosyl transfer mechanism, including essential roles of a histidine (general base) and two tyrosine residues (coordination of the phosphate leaving group). This work provides a framework for understanding the activity of several sialyltransferases, from bacterial to human, and for the structure-based design of specific inhibitors.
About this Structure
1RO7 is a Single protein structure of sequence from Campylobacter jejuni with and as ligands. Full crystallographic information is available from OCA.
Reference
Structural analysis of the sialyltransferase CstII from Campylobacter jejuni in complex with a substrate analog., Chiu CP, Watts AG, Lairson LL, Gilbert M, Lim D, Wakarchuk WW, Withers SG, Strynadka NC, Nat Struct Mol Biol. 2004 Feb;11(2):163-70. Epub 2004 Jan 18. PMID:14730352
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