PDBsum entry 5cc7

Transferase

PDB id: 5cc7

Contents

Protein chain

704 a.a.

Ligands

1F1

Metals

_MG

Waters ×726

References listed in PDB file

Key reference

Title

Crystal structures of fragment-Bound malate synthase mycobacterium tuberculosis provide insights into mech and potential inhibitor designs

Authors

H.-L.Huang, I.V.Krieger, V.B.Gawandi, M.Parai, J.C.Sacche.

Ref.

TO BE PUBLISHED ...

Secondary reference #1

Title

Biochemical and structural studies of malate synthase from mycobacterium tuberculosis.

Authors

C.V.Smith, C.C.Huang, A.Miczak, D.G.Russell, J.C.Sacchettini, K.Höner zu bentrup.

Ref.

J Biol Chem, 2003, 278, 1735-1743. [DOI no: 10.1074/jbc.M209248200]

PubMed id

12393860

Figure 2.
Fig. 2. a, simulated-annealing omitted F[o] F[c] map of coenzyme A. The map was contoured at 3 sigma. b, the interactions between coenzyme A and GlcB. The coenzyme A is shown in white, and the carbons of the interacting amino acids are in gold. The malate and magnesium ion in the active site are also shown. c, binding of coenzyme A to the active site of GlcB. Surfaces were made around the protein atoms and colored according to the electrostatic potential, red for acidic, and blue for basic residues, and were made using the program SPOCK (66). Mg2+ in the active site is shown as a blue sphere.

Figure 3.
Fig. 3. a, active site of the GlcB-glyoxylate binary complex. Mg2+ is held in an octahedral coordination by the carboxylate side chains of Glu-434 and Asp-462, one carboxylate oxygen, one aldehyde oxygen of glyoxylate- and two water molecules. b, active site of GlcB-malate-CoA ternary complex. A water molecule that is seen coordinating Mg2+ in GlcB-glyoxylate is replaced by the hydroxyl of malate.

The above figures are reproduced from the cited reference with permission from the ASBMB

Secondary reference #2

Title

Structure-Guided discovery of phenyl-Diketo acids as potent inhibitors of m. Tuberculosis malate synthase.

Authors

I.V.Krieger, J.S.Freundlich, V.B.Gawandi, J.P.Roberts, V.B.Gawandi, Q.Sun, J.L.Owen, M.T.Fraile, S.I.Huss, J.L.Lavandera, T.R.Ioerger, J.C.Sacchettini.

Ref.

Chem Biol, 2012, 19, 1556-1567.

PubMed id

23261599