PDBsum entry 1vq3

Ligase

PDB id: 1vq3

Contents

Protein chains

86 a.a. *

Waters ×301

* Residue conservation analysis

PDB id:

1vq3

Name:

Ligase

Title:

Crystal structure of phosphoribosylformylglycinamidine synthase, purs subunit (ec 6.3.5.3) (tm1244) from thermotoga maritima at 1.90 a resolution

Structure:

Phosphoribosylformylglycinamidine synthase, purs subunit. Chain: a, b, c, d. Engineered: yes

Source:

Thermotoga maritima. Organism_taxid: 243274. Strain: msb8. Gene: tm1244. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Tetramer (from PQS)

Resolution:

1.90Å R-factor: 0.180 R-free: 0.235

Authors:

Joint Center For Structural Genomics (Jcsg)

Key ref:

I.I.Mathews et al. (2006). Crystal structure of phosphoribosylformyl-glycinamidine synthase II, PurS subunit (TM1244) from Thermotoga maritima at 1.90 A resolution. Proteins, 65, 249-254. PubMed id: 16865708 DOI: 10.1002/prot.21024

Date:

15-Dec-04 Release date: 28-Dec-04

Protein chains

Q9X0X1  (PURS_THEMA) -  Phosphoribosylformylglycinamidine synthase subunit PurS from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)

Seq: 82 a.a.

Struc: 86 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.6.3.5.3 - phosphoribosylformylglycinamidine synthase.
• Pathway: Purine Biosynthesis (early stages)
• Reaction: N₂-formyl-N₁-(5-phospho-beta-D-ribosyl)glycinamide + L-glutamine + ATP + H2O = 2-formamido-N₁-(5-O-phospho-beta-D-ribosyl)acetamidine + L-glutamate + ADP + phosphate + H⁺

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1002/prot.21024

Proteins 65:249-254 (2006)

PubMed id: 16865708

Crystal structure of phosphoribosylformyl-glycinamidine synthase II, PurS subunit (TM1244) from Thermotoga maritima at 1.90 A resolution.

I.I.Mathews, S.S.Krishna, R.Schwarzenbacher, D.McMullan, L.Jaroszewski, M.D.Miller, P.Abdubek, S.Agarwalla, E.Ambing, H.L.Axelrod, J.M.Canaves, D.Carlton, H.J.Chiu, T.Clayton, M.DiDonato, L.Duan, M.A.Elsliger, S.K.Grzechnik, J.Hale, E.Hampton, J.Haugen, K.K.Jin, H.E.Klock, E.Koesema, J.S.Kovarik, A.Kreusch, P.Kuhn, I.Levin, A.T.Morse, E.Nigoghossian, L.Okach, S.Oommachen, J.Paulsen, K.Quijano, R.Reyes, C.L.Rife, G.Spraggon, R.C.Stevens, H.van den Bedem, A.White, G.Wolf, Q.Xu, K.O.Hodgson, J.Wooley, A.M.Deacon, A.Godzik, S.A.Lesley, I.A.Wilson.

ABSTRACT

No abstract given.

Selected figure(s)

Figure 2.
Figure 2. Domain delineation of PurS. (A) Structural representative of the ferredoxin-like fold: the anticodon-binding domain of PheRS (PDB code: 1pys, chain B). (B) Dimeric unit of PurS colored according to chains (chain A: blue, chain B: red). The PurS domain-swapped dimer structure contains two domains (separated by a black horizontal bar), each of which resembles the ferredoxin-like fold. The ferredoxin-like fold is made of four -strands and two -helices, and in PurS these structural elements are contributed from the two chains of the dimer by a domain swap of -helix H1 and -strand 2. The elements are labeled according to the ferredoxin-like fold.

Figure 3.
Figure 3. (A) Structural alignment of PurS (blue) with the N-terminal domain of lgPurL (gray) from S. typhimurium C[ ]atoms from the dimer of TM1244 were used for the alignment with lgPurL. The largest structural difference corresponds to strand 3 of chain A, which is replaced by a long loop (see arrow) that acts as a linker between the adjacent PurS-like domains in lgPurL. (B) Stereo ribbon diagram of a superposition of lgPurL from S. typhimurium (FGAR-AT; gray) with PurS (TM1244; blue) and smPurL (TM1246; orange). Ligands of lgPurL are shown as CPK (Corey, Pauling, and Kultun) color scheme. The arrow indicates the expected location of the PurQ protein (TM1245) in FGAR-AT from T. maritima.

The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2006, 65, 249-254) copyright 2006.

Figures were selected by an automated process.