2hxw
From Proteopedia
(New page: 200px<br /><applet load="2hxw" size="350" color="white" frame="true" align="right" spinBox="true" caption="2hxw, resolution 1.60Å" /> '''Crystal Structure of...) |
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==Overview== | ==Overview== | ||
| - | Campylobacter jejuni is unusual among bacteria in possessing a | + | 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== | ==About this Structure== | ||
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[[Category: Campylobacter jejuni]] | [[Category: Campylobacter jejuni]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: BSGI, Montreal-Kingston | + | [[Category: BSGI, Montreal-Kingston Bacterial Structural Genomics Initiative.]] |
[[Category: Bhatia, S.]] | [[Category: Bhatia, S.]] | ||
[[Category: Cygler, M.]] | [[Category: Cygler, M.]] | ||
[[Category: Matte, A.]] | [[Category: Matte, A.]] | ||
[[Category: Munger, C.]] | [[Category: Munger, C.]] | ||
| - | [[Category: Rangarajan, E | + | [[Category: Rangarajan, E S.]] |
| - | [[Category: Watson, D | + | [[Category: Watson, D C.]] |
| - | [[Category: Young, N | + | [[Category: Young, N M.]] |
[[Category: FLC]] | [[Category: FLC]] | ||
[[Category: bsgi]] | [[Category: bsgi]] | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:46:59 2008'' |
Revision as of 15:47, 21 February 2008
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Crystal Structure of Peb3 from Campylobacter jejuni
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.
About this Structure
2HXW is a Single protein structure of sequence from Campylobacter jejuni with as ligand. Full crystallographic information is available from OCA.
Reference
Structural context for protein N-glycosylation in bacteria: The structure of PEB3, an adhesin from Campylobacter jejuni., Rangarajan ES, Bhatia S, Watson DC, Munger C, Cygler M, Matte A, Young NM, Protein Sci. 2007 May;16(5):990-5. PMID:17456748
Page seeded by OCA on Thu Feb 21 17:46:59 2008
Categories: Campylobacter jejuni | Single protein | BSGI, Montreal-Kingston Bacterial Structural Genomics Initiative. | Bhatia, S. | Cygler, M. | Matte, A. | Munger, C. | Rangarajan, E S. | Watson, D C. | Young, N M. | FLC | Bsgi | Montreal-kingston bacterial structural genomics initiative | N-glycosylation | Peb3 | Periplasmic binding protein | Structural genomics
