2hxw: Difference between revisions

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==Overview==

Campylobacter jejuni is unusual among bacteria in possessing a, eukaryotic-like system for N-linked protein glycosylation at Asn residues, in sequons of the type Asp/Glu-Xaa-Asn-Xaa-Ser/Thr. However, little is, known about the structural context of the glycosylated sequons, limiting, the design of novel recombinant glycoproteins. To obtain more information, on sequon structure, we have determined the crystal structure of the PEB3, (Cj0289c) dimer. PEB3 has the class II periplasmic-binding protein fold, with each monomer having two domains with a ligand-binding site containing, citrate located between them, and overall resembles molybdate- and, sulfate-binding proteins. The sequon around Asn90 is located within a, surface-exposed loop joining two structural elements. The three key, residues are well exposed on the surface; hence, they may be accessible to, the PglB oligosaccharyltransferase in the folded state.

Campylobacter jejuni is unusual among bacteria in possessing a eukaryotic-like system for N-linked protein glycosylation at Asn residues in sequons of the type Asp/Glu-Xaa-Asn-Xaa-Ser/Thr. However, little is known about the structural context of the glycosylated sequons, limiting the design of novel recombinant glycoproteins. To obtain more information on sequon structure, we have determined the crystal structure of the PEB3 (Cj0289c) dimer. PEB3 has the class II periplasmic-binding protein fold, with each monomer having two domains with a ligand-binding site containing citrate located between them, and overall resembles molybdate- and sulfate-binding proteins. The sequon around Asn90 is located within a surface-exposed loop joining two structural elements. The three key residues are well exposed on the surface; hence, they may be accessible to the PglB oligosaccharyltransferase in the folded state.

==About this Structure==

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[[Category: Campylobacter jejuni]]

[[Category: Single protein]]

[[Category: BSGI, Montreal-Kingston.Bacterial.Structural.Genomics.Initiative.]]

[[Category: BSGI, Montreal-Kingston Bacterial Structural Genomics Initiative.]]

[[Category: Bhatia, S.]]

[[Category: Cygler, M.]]

[[Category: Matte, A.]]

[[Category: Munger, C.]]

[[Category: Rangarajan, E.S.]]

[[Category: Rangarajan, E S.]]

[[Category: Watson, D.C.]]

[[Category: Watson, D C.]]

[[Category: Young, N.M.]]

[[Category: Young, N M.]]

[[Category: FLC]]

[[Category: bsgi]]

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[[Category: structural genomics]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-Campylobacter jejuni is unusual among bacteria in possessing a, eukaryotic-like system for N-linked protein glycosylation at Asn residues, in sequons of the type Asp/Glu-Xaa-Asn-Xaa-Ser/Thr. However, little is, known about the structural context of the glycosylated sequons, limiting, the design of novel recombinant glycoproteins. To obtain more information, on sequon structure, we have determined the crystal structure of the PEB3, (Cj0289c) dimer. PEB3 has the class II periplasmic-binding protein fold, with each monomer having two domains with a ligand-binding site containing, citrate located between them, and overall resembles molybdate- and, sulfate-binding proteins. The sequon around Asn90 is located within a, surface-exposed loop joining two structural elements. The three key, residues are well exposed on the surface; hence, they may be accessible to, the PglB oligosaccharyltransferase in the folded state.
+Campylobacter jejuni is unusual among bacteria in possessing a eukaryotic-like system for N-linked protein glycosylation at Asn residues in sequons of the type Asp/Glu-Xaa-Asn-Xaa-Ser/Thr. However, little is known about the structural context of the glycosylated sequons, limiting the design of novel recombinant glycoproteins. To obtain more information on sequon structure, we have determined the crystal structure of the PEB3 (Cj0289c) dimer. PEB3 has the class II periplasmic-binding protein fold, with each monomer having two domains with a ligand-binding site containing citrate located between them, and overall resembles molybdate- and sulfate-binding proteins. The sequon around Asn90 is located within a surface-exposed loop joining two structural elements. The three key residues are well exposed on the surface; hence, they may be accessible to the PglB oligosaccharyltransferase in the folded state.
 ==About this Structure==
@@ Line 13: / Line 13: @@
 [[Category: Campylobacter jejuni]]
 [[Category: Single protein]]
-[[Category: BSGI, Montreal-Kingston.Bacterial.Structural.Genomics.Initiative.]]
+[[Category: BSGI, Montreal-Kingston Bacterial Structural Genomics Initiative.]]
 [[Category: Bhatia, S.]]
 [[Category: Cygler, M.]]
 [[Category: Matte, A.]]
 [[Category: Munger, C.]]
-[[Category: Rangarajan, E.S.]]
+[[Category: Rangarajan, E S.]]
-[[Category: Watson, D.C.]]
+[[Category: Watson, D C.]]
-[[Category: Young, N.M.]]
+[[Category: Young, N M.]]
 [[Category: FLC]]
 [[Category: bsgi]]
@@ Line 29: / Line 29: @@
 [[Category: structural genomics]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:27:19 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:46:59 2008''