6ACN
STRUCTURE OF ACTIVATED ACONITASE. FORMATION OF THE (4FE-4S) CLUSTER IN THE CRYSTAL
Summary for 6ACN
Entry DOI | 10.2210/pdb6acn/pdb |
Descriptor | ACONITASE, SULFATE ION, IRON/SULFUR CLUSTER, ... (5 entities in total) |
Functional Keywords | lyase(carbon-oxygen) |
Biological source | Sus scrofa (pig) |
Total number of polymer chains | 1 |
Total formula weight | 83412.87 |
Authors | Robbins, A.H.,Stout, C.D. (deposition date: 1990-01-16, release date: 1990-07-15, Last modification date: 2024-10-23) |
Primary citation | Robbins, A.H.,Stout, C.D. Structure of activated aconitase: formation of the [4Fe-4S] cluster in the crystal. Proc.Natl.Acad.Sci.USA, 86:3639-3643, 1989 Cited by PubMed Abstract: The structure of activated pig heart aconitase [citrate(isocitrate) hydro-lyase, EC 4.2.1.3] containing a [4Fe-4S] cluster has been refined at 2.5-A resolution to a crystallographic residual of 18.2%. Comparison of this structure to the recently determined 2.1-A resolution structure of the inactive enzyme containing a [3Fe-4S] cluster, by difference Fourier analysis, shows that upon activation iron is inserted into the structure isomorphously. The common atoms of the [3Fe-4S] and [4Fe-4S] cores agree within 0.1 A; the three common cysteinyl S gamma ligand atoms agree within 0.25 A. The fourth ligand of the Fe inserted into the [3Fe-4S] cluster is a water or hydroxyl from solvent, consistent with the absence of a free cysteine ligand in the enzyme active site cleft and the isomorphism of the two structures. A water molecule occupies a similar site in the crystal structure of the inactive enzyme. PubMed: 2726740DOI: 10.1073/pnas.86.10.3639 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
Download full validation report
