scholarly journals Crystal structure of the Campylobacter jejuni Cj0090 protein reveals a novel variant of the immunoglobulin fold among bacterial lipoproteins

2012 ◽  
Vol 80 (12) ◽  
pp. 2804-2809
Author(s):  
Seonghee Paek ◽  
Fumihiro Kawai ◽  
Kyoung-Jae Choi ◽  
Hye-Jeong Yeo
Keyword(s):  
Crystal Structure ◽  
Campylobacter Jejuni ◽  
Novel Variant ◽  
Immunoglobulin Fold

Crystal structure of Ca2Ln3Sb3O14 (Ln=La, Pr, Nd and Y): A novel variant of weberite

2007 ◽  
Vol 180 (11) ◽  
pp. 3166-3171 ◽  
Author(s):  
Y.S. Au ◽  
W.T. Fu ◽  
D.J.W. IJdo
Keyword(s):  
Crystal Structure ◽  
Novel Variant

scholarly journals Crystal Structure of the Transcriptional Regulator CmeR from Campylobacter jejuni

2007 ◽  
Vol 372 (3) ◽  
pp. 583-593 ◽  
Author(s):  
Ruoyu Gu ◽  
Chih-Chia Su ◽  
Feng Shi ◽  
Ming Li ◽  
Gerry McDermott ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Campylobacter Jejuni ◽  
Transcriptional Regulator

scholarly journals Crystal structure of virulence factor CJ0248 from Campylobacter jejuni at 2.25 Å resolution reveals a new fold

2005 ◽  
Vol 62 (1) ◽  
pp. 292-296 ◽  
Author(s):  
Qingping Xu ◽  
Robert Schwarzenbacher ◽  
Daniel McMullan ◽  
Polat Abdubek ◽  
Sanjay Agarwalla ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Campylobacter Jejuni ◽  
Virulence Factor

Crystal structure of chaperone protein PapD reveals an immunoglobulin fold

Nature ◽  
1989 ◽  
Vol 342 (6247) ◽  
pp. 248-251 ◽  
Author(s):  
Anders Holmgren ◽  
Carl-Lvar Bränden
Keyword(s):  
Crystal Structure ◽  
Chaperone Protein ◽  
Immunoglobulin Fold

scholarly journals Hexameric Assembly of the Bifunctional Methylerythritol 2,4-Cyclodiphosphate Synthase and Protein-Protein Associations in the Deoxy-xylulose-dependent Pathway of Isoprenoid Precursor Biosynthesis

2004 ◽  
Vol 279 (50) ◽  
pp. 52753-52761 ◽  
Author(s):  
Mads Gabrielsen ◽  
Charles S. Bond ◽  
Irene Hallyburton ◽  
Stefan Hecht ◽  
Adelbert Bacher ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Escherichia Coli ◽  
Enzyme Activity ◽  
Agrobacterium Tumefaciens ◽  
Complex Formation ◽  
Campylobacter Jejuni ◽  
Biosynthetic Pathway ◽  
Bacterial Pathogen ◽  
The Core ◽  
Dependent Pathway

The bifunctional methylerythritol 4-phosphate cytidylyltransferase methylerythritol 2,4-cyclodiphosphate synthase (IspDF) is unusual in that it catalyzes nonconsecutive reactions in the 1-deoxy-d-xylulose 5-phosphate (DOXP) pathway of isoprenoid precursor biosynthesis. The crystal structure of IspDF from the bacterial pathogenCampylobacter jejunireveals an elongated hexamer withD3symmetry compatible with the dimeric 2C-methyl-d-erythritol-4-phosphate cytidylyltransferase and trimeric 2C-methyl-d-erythritol-2,4-cyclodiphosphate synthase monofunctional enzymes. Complex formation of IspDF with 4-diphosphocytidyl-2C-methyl-d-erythritol kinase (IspE), the intervening enzyme activity in the pathway, has been observed in solution for the enzymes fromC. jejuniandAgrobacterium tumefaciens. The monofunctional enzymes (2C-methyl-d-erythritol-4-phosphate cytidylyltransferase, IspE, and 2C-methyl-d-erythritol-2,4-cyclodiphosphate synthase) involved in the DOXP biosynthetic pathway ofEscherichia colialso show physical associations. We propose that complex formation of the three enzymes at the core of the DOXP pathway can produce an assembly localizing 18 catalytic centers for the early stages of isoprenoid biosynthesis.

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