4DCB

Y. pestis Plasminogen Activator Pla in Complex with Human Plasminogen Activation Loop Peptide ALP11

This is a non-PDB format compatible entry.

Summary for 4DCB

• Entry DOI: 10.2210/pdb4dcb/pdb
• Descriptor: Coagulase/fibrinolysin, Plasminogen, (4R)-2-METHYLPENTANE-2,4-DIOL, ... (7 entities in total)
• Functional Keywords: beta barrel, plasminogen activator, protease, outer membrane, hydrolase
• Biological source: Yersinia pestis; More
• Cellular location: Cell outer membrane; Multi-pass membrane protein (By similarity): P17811; Secreted: P00747
• Total number of polymer chains: 2
• Total formula weight: 35498.15

Authors

Eren, E.,van den Berg, B. (deposition date: 2012-01-17, release date: 2012-06-06, Last modification date: 2024-11-27)

Primary citation

Eren, E.,van den Berg, B.
Structural basis for activation of an integral membrane protease by lipopolysaccharide.
J.Biol.Chem., 287:23971-23976, 2012

PubMed Abstract: Omptins constitute a unique family of outer membrane proteases that are widespread in Enterobacteriaceae. The plasminogen activator (Pla) of Yersinia pestis is an omptin family member that is very important for development of both bubonic and pneumonic plague. The physiological function of Pla is to cleave (activate) human plasminogen to form the plasma protease plasmin. Uniquely, lipopolysaccharide (LPS) is essential for the catalytic activity of all omptins, including Pla. Why omptins require LPS for enzymatic activity is unknown. Here, we report the co-crystal structure of LPS-free Pla in complex with the activation loop peptide of human plasminogen, its natural substrate. The structure shows that in the absence of LPS, the peptide substrate binds deep within the active site groove and displaces the nucleophilic water molecule, providing an explanation for the dependence of omptins on LPS for enzymatic activity.

PubMed: 22645135
DOI: 10.1074/jbc.M112.376418

Experimental method

X-RAY DIFFRACTION (2.033 Å)