PDBsum entry: 1zcz

Transferase/hydrolase

PDB id: 1zcz

Contents

Protein chains

452 a.a. *

Ligands

PG4 ×2

Metals

__K ×2

Waters ×636

* Residue conservation analysis

PDB id:

1zcz

Name:

Transferase/hydrolase

Title:

Crystal structure of phosphoribosylaminoimidazolecarboxamide formyltransferase / imp cyclohydrolase (tm1249) from thermo maritima at 1.88 a resolution

Structure:

Bifunctional purine biosynthesis protein purh. Chain: a, b. Synonym: phosphoribosylaminoimidazolecarboxamide formyltran imp cyclohydrolase. Engineered: yes. Mutation: yes

Source:

Thermotoga maritima. Organism_taxid: 2336. Gene: purh. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Dimer (from PQS)

Resolution:

1.88Å R-factor: 0.158 R-free: 0.197

Authors:

Joint Center For Structural Genomics (Jcsg)

Key ref:

H.L.Axelrod et al. (2008). Crystal structure of AICAR transformylase IMP cyclohydrolase (TM1249) from Thermotoga maritima at 1.88 A resolution. Proteins, 71, 1042-1049. PubMed id: 18260100 DOI: 10.1002/prot.21967

Date:

13-Apr-05 Release date: 26-Apr-05

Protein chains

Q9X0X6  (PUR9_THEMA) -  Bifunctional purine biosynthesis protein PurH

Seq: 452 a.a.

Struc: 452 a.a.

Enzyme reactions

• Enzyme class 1: E.C.2.1.2.3 - Phosphoribosylaminoimidazolecarboxamide formyltransferase.
• Pathway: Purine Biosynthesis (late stages)
• Reaction: 10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4- carboxamide = tetrahydrofolate + 5-formamido-1-(5-phospho-D- ribosyl)imidazole-4-carboxamide
• Enzyme class 2: E.C.3.5.4.10 - Imp cyclohydrolase.

Pathway:

• Reaction: IMP + H₂O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

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

 Gene Ontology (GO) functional annotation 

• Biological process: metabolic process (3 terms)
• Biochemical function: catalytic activity (5 terms)

reference

DOI no: 10.1002/prot.21967

Proteins 71:1042-1049 (2008)

PubMed id: 18260100

Crystal structure of AICAR transformylase IMP cyclohydrolase (TM1249) from Thermotoga maritima at 1.88 A resolution.

H.L.Axelrod, D.McMullan, S.S.Krishna, M.D.Miller, M.A.Elsliger, P.Abdubek, E.Ambing, T.Astakhova, D.Carlton, H.J.Chiu, T.Clayton, L.Duan, J.Feuerhelm, S.K.Grzechnik, J.Hale, G.W.Han, J.Haugen, L.Jaroszewski, K.K.Jin, H.E.Klock, M.W.Knuth, E.Koesema, A.T.Morse, E.Nigoghossian, L.Okach, S.Oommachen, J.Paulsen, K.Quijano, R.Reyes, C.L.Rife, H.van den Bedem, D.Weekes, 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. The biologically relevant dimer of PurH from Thermotoga maritima, and a shift in the relative orientation of the two functional regions of TM1249 compared to the avian enzyme. A: Stereo ribbon diagram of the dimer of TM1249 showing the locations of the IMPCH and AICAR Tfase regions. The active sites of IMPCH and AICAR Tfase are labeled with cyan and orange asterisks, respectively. Bound K+ atoms are shown as spheres (grey) and PEG molecules as sticks (pink) (B) (Left) The relative shift in orientation between the N-terminal IMPCH domain of TM1249 (blue) and that of the avian enzyme (grey) (PDB accession code: 1m9n). (Right) FATCAT-optimized alignment of the N- and C-terminal regions of the avian enzyme and TM1249 after implementing a 90° twist in the hinge region of TM1249. A monomer of the avian protein is shown in grey, the N-terminal domain of TM1249 is in green, and the C-terminal domains of TM1249 are in red.

Figure 3.
Figure 3. The active sites of PurH from Thermotoga maritima. A: Stereo diagram of residues in the putative IMPCH active site of TM1249 superimposed on the avian structure (PDB ID: 1m9n). The carbon atoms on the side chains of TM1249 are shown in green, while the carbon atoms on the active site ligand (XMP) and on the side chains of the avian enzyme are in cyan. Residues from the avian enzyme are shown in parentheses. The side chain of Lys 11 in TM1249 is disordered and, consequently, only the carbon atom is shown. The location of XMP, an inhibitor of IMPCH, from the avian crystal structure is shown. B: Stereo diagram of residues in the putative AICAR Tfase active site of TM1249 superimposed on the avian structure, with the same color and labeling scheme used in (A). The AICAR substrate is from the avian structure.

The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2008, 71, 1042-1049) copyright 2008.

Figures were selected by an automated process.