Structure of the catalytic trimer of<i>Methanococcus jannaschii</i>aspartate transcarbamoylase in an orthorhombic crystal form

Vitali, Jacqueline; Colaneri, Michael J.

doi:10.1107/s1744309108025359

Cited by 2 publications

(2 citation statements)

References 27 publications

(39 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Three are structures of the isolated catalytic trimer [ 40 , 41 ]. Seventeen structures are from organisms other than E. coli , six are from the hyperthermophilic archaeons, Pyrococcus abyssi [ 42 ], Sulfolobus acidocaldarius [ 43 , 44 ] and Methanococcus jannaschii [ 45 , 46 , 47 ], and one is from the γ-division of proteobacteria Moritella profunda , a psychrophilic deep sea bacterium [ 48 ]. S. acidocaldarius ATCase was solved as the dodecameric holoenzyme, while the structure from P. abyssi is of the catalytic trimer complexed with the bisubstrate analogue, N -phosphonacetyl- l -aspartate (PALA).…”

Section: Structures Deposited In the Protein Data Bank (Pdb)mentioning

confidence: 99%

From Genome to Structure and Back Again: A Family Portrait of the Transcarbamylases

Shi

Allewell

Tuchman

2015

IJMS

View full text Add to dashboard Cite

Enzymes in the transcarbamylase family catalyze the transfer of a carbamyl group from carbamyl phosphate (CP) to an amino group of a second substrate. The two best-characterized members, aspartate transcarbamylase (ATCase) and ornithine transcarbamylase (OTCase), are present in most organisms from bacteria to humans. Recently, structures of four new transcarbamylase members, N-acetyl-l-ornithine transcarbamylase (AOTCase), N-succinyl-l-ornithine transcarbamylase (SOTCase), ygeW encoded transcarbamylase (YTCase) and putrescine transcarbamylase (PTCase) have also been determined. Crystal structures of these enzymes have shown that they have a common overall fold with a trimer as their basic biological unit. The monomer structures share a common CP binding site in their N-terminal domain, but have different second substrate binding sites in their C-terminal domain. The discovery of three new transcarbamylases, l-2,3-diaminopropionate transcarbamylase (DPTCase), l-2,4-diaminobutyrate transcarbamylase (DBTCase) and ureidoglycine transcarbamylase (UGTCase), demonstrates that our knowledge and understanding of the spectrum of the transcarbamylase family is still incomplete. In this review, we summarize studies on the structures and function of transcarbamylases demonstrating how structural information helps to define biological function and how small structural differences govern enzyme specificity. Such information is important for correctly annotating transcarbamylase sequences in the genome databases and for identifying new members of the transcarbamylase family.

show abstract

Section: Structures Deposited In the Protein Data Bank (Pdb)mentioning

confidence: 99%

From Genome to Structure and Back Again: A Family Portrait of the Transcarbamylases

Shi

Allewell

Tuchman

2015

IJMS

View full text Add to dashboard Cite

show abstract

“…Currently, the crystal structures of bacterial ATCases from Escherichia coli (Honzatko et al, 1982), Bacillus subtilis (Stevens et al, 1991), Pyrococcus abyssi (Van Boxstael et al, 2003), Sulfolobus acidocaldarius, Moritella profunda (De Vos et al, 2004, 2007 and Methanococcus jannaschii (Vitali & Colaneri, 2008), and of the A. aeolicus ATCase-DHO complex (Zhang et al, 2009) have been reported. In the present study, we report the expression, purification, crystallization and preliminary X-ray analysis of TcATCase.…”

Section: Introductionmentioning

confidence: 99%

Crystallization and preliminary X-ray analysis of aspartate transcarbamoylase from the parasitic protistTrypanosoma cruzi

et al. 2009

View full text Add to dashboard Cite

Aspartate transcarbamoylase (ATCase), the second enzyme of the de novo pyrimidine-biosynthetic pathway, catalyzes the production of carbamoyl aspartate from carbamoyl phosphate and L-aspartate. In contrast to Escherichia coli ATCase and eukaryotic CAD multifunctional fusion enzymes, Trypanosoma cruzi ATCase lacks regulatory subunits and is not part of the multifunctional fusion enzyme. Recombinant T. cruzi ATCase expressed in E. coli was purified and crystallized in a ligand-free form and in a complex with carbamoyl phosphate at 277 K by the sitting-drop vapour-diffusion technique using polyethylene glycol 3350 as a precipitant. Ligand-free crystals (space group P1, unit-cell parameters a = 78.42, b = 79.28, c = 92.02 A, alpha = 69.56, beta = 82.90, gamma = 63.25 degrees) diffracted X-rays to 2.8 A resolution, while those cocrystallized with carbamoyl phosphate (space group P2(1), unit-cell parameters a = 88.41, b = 158.38, c = 89.00 A, beta = 119.66 degrees) diffracted to 1.6 A resolution. The presence of two homotrimers in the asymmetric unit (38 kDa x 6) gives V(M) values of 2.3 and 2.5 A(3) Da(-1) for the P1 and P2(1) crystal forms, respectively.

show abstract

Structure of the catalytic trimer ofMethanococcus jannaschiiaspartate transcarbamoylase in an orthorhombic crystal form

Cited by 2 publications

References 27 publications

From Genome to Structure and Back Again: A Family Portrait of the Transcarbamylases

From Genome to Structure and Back Again: A Family Portrait of the Transcarbamylases

Crystallization and preliminary X-ray analysis of aspartate transcarbamoylase from the parasitic protistTrypanosoma cruzi

Contact Info

Product

Resources

About