Crystal Structure of Dephospho-Coenzyme A Kinase from Haemophilus influenzae

2001 ◽  
Vol 136 (2) ◽  
pp. 119-125 ◽  
Author(s):  
Galina Obmolova ◽  
Alexey Teplyakov ◽  
Nicklas Bonander ◽  
Edward Eisenstein ◽  
Andrew J Howard ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Haemophilus Influenzae ◽  
Coenzyme A

The 1.75 Å Crystal Structure of Acetyl-CoA Synthetase Bound to Adenosine-5‘-propylphosphate and Coenzyme A†

Biochemistry ◽  
2003 ◽  
Vol 42 (10) ◽  
pp. 2866-2873 ◽  
Author(s):  
Andrew M. Gulick ◽  
Vincent J. Starai ◽  
Alexander R. Horswill ◽  
Kristen M. Homick ◽  
Jorge C. Escalante-Semerena
Keyword(s):  
Crystal Structure ◽  
Coenzyme A ◽  
Acetyl Coa

scholarly journals Crystal structure of FadR, a fatty acid-responsive transcription factor with a novel acyl coenzyme A-binding fold

2000 ◽  
Vol 19 (19) ◽  
pp. 5167-5177 ◽  
Author(s):  
D.M.F van Aalten ◽  
C.C. DiRusso ◽  
J. Knudsen ◽  
R.K. Wierenga
Keyword(s):  
Crystal Structure ◽  
Transcription Factor ◽  
Fatty Acid ◽  
Coenzyme A ◽  
Acyl Coenzyme A

scholarly journals Crystal Structure of Methylmalonyl-Coenzyme A Epimerase from P. shermanii

Structure ◽  
2001 ◽  
Vol 9 (7) ◽  
pp. 637-646 ◽  
Author(s):  
Andrew A McCarthy ◽  
Heather M Baker ◽  
Steven C Shewry ◽  
Mark L Patchett ◽  
Edward N Baker
Keyword(s):  
Crystal Structure ◽  
Coenzyme A

scholarly journals How coenzyme B12 radicals are generated: the crystal structure of methylmalonyl-coenzyme A mutase at 2 å resolution

Structure ◽  
1996 ◽  
Vol 4 (3) ◽  
pp. 339-350 ◽  
Author(s):  
Filippo Mancia ◽  
Nicholas H Keep ◽  
Atsushi Nakagawa ◽  
Peter F Leadlay ◽  
Sean McSweeney ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Coenzyme A ◽  
Coenzyme B12

Crystal Structure of Tabtoxin Resistance Protein Complexed with Acetyl Coenzyme A Reveals the Mechanism for β-Lactam Acetylation

2003 ◽  
Vol 325 (5) ◽  
pp. 1019-1030 ◽  
Author(s):  
Hongzhen He ◽  
Yi Ding ◽  
Mark Bartlam ◽  
Fei Sun ◽  
Yi Le ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Coenzyme A ◽  
Acetyl Coenzyme A ◽  
Acetyl Coenzyme ◽  
Resistance Protein

scholarly journals Crystal Structure of TDP-Fucosamine Acetyltransferase (WecD) from Escherichia coli, an Enzyme Required for Enterobacterial Common Antigen Synthesis

2006 ◽  
Vol 188 (15) ◽  
pp. 5606-5617 ◽  
Author(s):  
Ming-Ni Hung ◽  
Erumbi Rangarajan ◽  
Christine Munger ◽  
Guy Nadeau ◽  
Traian Sulea ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Escherichia Coli ◽  
Coenzyme A ◽  
Structural Data ◽  
Enteric Bacteria ◽  
Common Antigen ◽  
Acetyl Coa ◽  
Enterobacterial Common Antigen ◽  
Thiolate Anion ◽  
Acetyl Transfer

ABSTRACT Enterobacterial common antigen (ECA) is a polysaccharide found on the outer membrane of virtually all gram-negative enteric bacteria and consists of three sugars, N-acetyl-d-glucosamine, N-acetyl-d-mannosaminuronic acid, and 4-acetamido-4,6-dideoxy-d-galactose, organized into trisaccharide repeating units having the sequence →3)-α-d-Fuc4NAc-(1→4)-β-d-ManNAcA-(1→4)-α-d-GlcNAc-(1→. While the precise function of ECA is unknown, it has been linked to the resistance of Shiga-toxin-producing Escherichia coli (STEC) O157:H7 to organic acids and the resistance of Salmonella enterica to bile salts. The final step in the synthesis of 4-acetamido-4,6-dideoxy-d-galactose, the acetyl-coenzyme A (CoA)-dependent acetylation of the 4-amino group, is carried out by TDP-fucosamine acetyltransferase (WecD). We have determined the crystal structure of WecD in apo form at a 1.95-Å resolution and bound to acetyl-CoA at a 1.66-Å resolution. WecD is a dimeric enzyme, with each monomer adopting the GNAT N-acetyltransferase fold, common to a number of enzymes involved in acetylation of histones, aminoglycoside antibiotics, serotonin, and sugars. The crystal structure of WecD, however, represents the first structure of a GNAT family member that acts on nucleotide sugars. Based on this cocrystal structure, we have used flexible docking to generate a WecD-bound model of the acetyl-CoA-TDP-fucosamine tetrahedral intermediate, representing the structure during acetyl transfer. Our structural data show that WecD does not possess a residue that directly functions as a catalytic base, although Tyr208 is well positioned to function as a general acid by protonating the thiolate anion of coenzyme A.

Crystal structure of human stearoyl–coenzyme A desaturase in complex with substrate

2015 ◽  
Vol 22 (7) ◽  
pp. 581-585 ◽  
Author(s):  
Hui Wang ◽  
Michael G Klein ◽  
Hua Zou ◽  
Weston Lane ◽  
Gyorgy Snell ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Coenzyme A
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