PDBsum entry 1o5h

Lyase

PDB id: 1o5h

Contents

Protein chains

200 a.a. *

* Residue conservation analysis

PDB id:

1o5h

Name:

Lyase

Title:

Crystal structure of formiminotetrahydrofolate cyclodeaminase (tm1560) from thermotoga maritima at 2.80 a resolution

Structure:

Formiminotetrahydrofolate cyclodeaminase. Chain: a, b. Engineered: yes

Source:

Thermotoga maritima. Organism_taxid: 2336. Gene: tm1560. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Dimer (from PQS)

Resolution:

2.80Å R-factor: 0.203 R-free: 0.278

Authors:

Joint Center For Structural Genomics (Jcsg)

Key ref:

Q.Xu et al. (2005). Crystal structure of a formiminotetrahydrofolate cyclodeaminase (TM1560) from Thermotoga maritima at 2.80 A resolution reveals a new fold. Proteins, 58, 976-981. PubMed id: 15651027 DOI: 10.1002/prot.20364

Date:

17-Sep-03 Release date: 30-Sep-03

Protein chains

Q9X1P6  (Q9X1P6_THEMA) -  Serine cycle enzyme, putative from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)

Seq: 202 a.a.

Struc: 200 a.a.

Enzyme reactions

• Enzyme class: E.C.4.3.1.4 - formimidoyltetrahydrofolate cyclodeaminase.
• Pathway: Folate Coenzymes
• Reaction: 5-formimidoyltetrahydrofolate + 2 H⁺ = (6R)-5,10- methenyltetrahydrofolate + NH4⁺

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

Key reference

DOI no: 10.1002/prot.20364

Proteins 58:976-981 (2005)

PubMed id: 15651027

Crystal structure of a formiminotetrahydrofolate cyclodeaminase (TM1560) from Thermotoga maritima at 2.80 A resolution reveals a new fold.

Q.Xu, R.Schwarzenbacher, D.McMullan, P.Abdubek, E.Ambing, T.Biorac, J.M.Canaves, H.J.Chiu, X.Dai, A.M.Deacon, M.DiDonato, M.A.Elsliger, A.Godzik, C.Grittini, S.K.Grzechnik, E.Hampton, M.Hornsby, L.Jaroszewski, H.E.Klock, E.Koesema, A.Kreusch, P.Kuhn, S.A.Lesley, I.Levin, M.D.Miller, A.Morse, K.Moy, J.Ouyang, R.Page, K.Quijano, R.Reyes, A.Robb, E.Sims, G.Spraggon, R.C.Stevens, H.van den Bedem, J.Velasquez, J.Vincent, F.von Delft, X.Wang, B.West, A.White, G.Wolf, O.Zagnitko, K.O.Hodgson, J.Wooley, I.A.Wilson.

ABSTRACT

No abstract given.

Selected figure(s)

Figure 1.
Figure 1. (A) Scheme for the reaction carried out by FTCD_CD (EC 4.3.1.4), which catalyzes the cyclization of the formimino group of N^5-formimidoyltetrahydrofolate, yielding N^5,N^10-methenyltetrahydrofolate and ammonia. (B) Crystal structure of TM1560. Ribbon diagram of T. maritima FTCD_CD color-coded from N-terminus (blue) to C-terminus (red) showing the domain organization. elices H1-H6 are indicated. (C) The TM1560 dimer view is shown along (above) and normal (below) to its two-fold axis. (D) Diagram showing the secondary structure elements in TM1560 superimposed on its primary sequence. The -helices, 3[10]-helices, -bulges, and -turns are indicated. Disordered regions are depicted by a dashed line with the corresponding sequence in brackets.

Figure 2.
Figure 2. (A) Superposition of TM1560 (gray) and invertase inhibitor Nt-Cif from Tobacco (PDB code: 1rj1, magenta). (B) The putative active site pocket in surface representation. Residues are colored according to sequence conservation, where green is conserved and white is nonconserved. The manually docked ligand N^5, N^10-methenyltetrahydrofolate (MTHF) is shown in stick representation (yellow). (C) Same orientation as (B), but shown in ribbon representation, with conserved residues in the putative active site of TM1560 and the manually docked MTHF ligand in stick representation. Monomers 1 and 2 in the dimer are shown in blue and gray, respectively.

The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2005, 58, 976-981) copyright 2005.