scholarly journals Crystal Structure of Type-III Geranylgeranyl Pyrophosphate Synthase fromSaccharomyces cerevisiaeand the Mechanism of Product Chain Length Determination

2006 ◽  
Vol 281 (21) ◽  
pp. 14991-15000 ◽  
Author(s):  
Tao-Hsin Chang ◽  
Rey-Ting Guo ◽  
Tzu-Ping Ko ◽  
Andrew H.-J. Wang ◽  
Po-Huang Liang
Keyword(s):  
Crystal Structure ◽  
Chain Length ◽  
Geranylgeranyl Pyrophosphate ◽  
Type Iii ◽  
Geranylgeranyl Pyrophosphate Synthase ◽  
Length Determination

scholarly journals Crystal Structure of Octaprenyl Pyrophosphate Synthase from HyperthermophilicThermotoga maritimaand Mechanism of Product Chain Length Determination

2003 ◽  
Vol 279 (6) ◽  
pp. 4903-4912 ◽  
Author(s):  
Rey-Ting Guo ◽  
Chih-Jung Kuo ◽  
Chia-Cheng Chou ◽  
Tzu-Ping Ko ◽  
Hui-Lin Shr ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Chain Length ◽  
Length Determination

scholarly journals The Crystal Structure of Human Geranylgeranyl Pyrophosphate Synthase Reveals a Novel Hexameric Arrangement and Inhibitory Product Binding

2006 ◽  
Vol 281 (31) ◽  
pp. 22004-22012 ◽  
Author(s):  
Kathryn L. Kavanagh ◽  
James E. Dunford ◽  
Gabor Bunkoczi ◽  
R. Graham G. Russell ◽  
Udo Oppermann
Keyword(s):  
Crystal Structure ◽  
Geranylgeranyl Pyrophosphate ◽  
Geranylgeranyl Pyrophosphate Synthase

Crystal structure of tandem type III fiibronectin domains from drosophila neuroglian at 2.0 å

Neuron ◽  
1994 ◽  
Vol 12 (4) ◽  
pp. 717-731 ◽  
Author(s):  
Andrew H. Huber ◽  
Yu-mei Eureka Wang ◽  
Allan J. Bieber ◽  
Pamela J. Bjorkman
Keyword(s):  
Crystal Structure ◽  
Type Iii

scholarly journals Chain Length Determination of Polyphosphates

1964 ◽  
Vol 47 (8) ◽  
pp. 920-921 ◽  
Author(s):  
S. Odagiri ◽  
T.A. Nickerson
Keyword(s):  
Chain Length ◽  
Length Determination

scholarly journals Structure of the human heterotetrameric cis-prenyltransferase complex

2020 ◽  
Author(s):  
Michal Lisnyansky Bar-El ◽  
Pavla Vankova ◽  
Petr Man ◽  
Yoni Haitin ◽  
Moshe Giladi
Keyword(s):  
Crystal Structure ◽  
Active Site ◽  
Substrate Binding ◽  
Synthesis Mechanism ◽  
Allosteric Communication ◽  
Pt Complex ◽  
C Terminus ◽  
Length Determination ◽  
Enzymatic Complex

AbstractThe human cis-prenyltransferase (hcis-PT) is an enzymatic complex essential for protein N-glycosylation. Synthesizing the precursor of the glycosyl carrier dolichol-phosphate, we reveal here that hcis-PT exhibits a novel heterotetrameric assembly in solution, composed of two catalytic dehydrodolichyl diphosphate synthase (DHDDS) and two inactive Nogo-B receptor (NgBR) subunits. The 2.3 Å crystal structure of the complex exposes a dimer-of-heterodimers arrangement, with DHDDS C-termini serving as homotypic assembly domains. Furthermore, the structure elucidates the molecular details associated with substrate binding, catalysis, and product length determination. Importantly, the distal C-terminus of NgBR transverses across the heterodimeric interface, directly participating in substrate binding and underlying the allosteric communication between the subunits. Finally, mapping disease-associated hcis-PT mutations involved in blindness, neurological and glycosylation disorders onto the structure reveals their clustering around the active site. Together, our structure of the hcis-PT complex unveils the dolichol synthesis mechanism and its perturbation in disease.

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