1L4Z

X-RAY CRYSTAL STRUCTURE OF THE COMPLEX OF MICROPLASMINOGEN WITH ALPHA DOMAIN OF STREPTOKINASE IN THE PRESENCE CADMIUM IONS

Summary for 1L4Z

• Entry DOI: 10.2210/pdb1l4z/pdb
• Related: 1BML 1BUI 1DDJ 1L4D 1QRZ
• Descriptor: Plasminogen, Streptokinase, CADMIUM ION, ... (4 entities in total)
• Functional Keywords: plasminogen, streptokinase, protein complex, hydrolase-blood clotting complex, hydrolase/blood clotting
• Biological source: Homo sapiens (human); More
• Cellular location: Secreted: P00747
• Total number of polymer chains: 2
• Total formula weight: 42759.41

Authors

Wakeham, N.,Terzyan, S.,Zhai, P.,Loy, J.A.,Tang, J.,Zhang, X.C. (deposition date: 2002-03-06, release date: 2002-12-11, Last modification date: 2024-10-16)

Primary citation

Wakeham, N.,Terzyan, S.,Zhai, P.,Loy, J.A.,Tang, J.,Zhang, X.C.
Effects of deletion of streptokinase residues 48-59 on plasminogen activation.
PROTEIN ENG., 15:753-761, 2002

PubMed Abstract: Streptokinase (SK) is a thrombolytic agent widely used for the clinical treatment of clotting disorders such as heart attack. The treatment is based on the ability of SK to bind plasminogen (Pg) or plasmin (Pm), forming complexes that proteolytically activate other Pg molecules to Pm, which carries out fibrinolysis. SK contains three major domains. The N-terminal domain, SKalpha, provides the complex with substrate recognition towards Pg. SKalpha contains a unique mobile loop, residues 45-70, absent in the corresponding domains of other bacterial Pg activators. To study the roles of this loop, we deleted 12 residues in this loop in both full-length SK and the SKalpha fragment. Kinetic data indicate that this loop participates in the recognition of substrate Pg, but does not function in the active site formation in the activator complex. Two crystal structures of the deletion mutant of SKalpha (SKalpha(delta)) complexed with the protease domain of Pg were determined. While the structure of SKalpha(delta) is essentially the same as this domain in full-length SK, the mode of SK-Pg interaction was however different from a previously observed structure. Even though mutagenesis studies indicated that the current complex represents a minor interacting form in solution, the binding to SKalpha(delta) triggered similar conformational changes in the Pg active site in both crystal forms.

PubMed: 12456874
DOI: 10.1093/protein/15.9.753

Experimental method

X-RAY DIFFRACTION (2.8 Å)