1ZLB

Crystal structure of catalytically-active phospholipase A2 in the absence of calcium

Summary for 1ZLB

• Entry DOI: 10.2210/pdb1zlb/pdb
• Related: 1UMV 1ZL7
• Descriptor: hypotensive phospholipase A2 (2 entities in total)
• Functional Keywords: asp49-pla2, toxin, snake venom, hydrolase
• Biological source: Bothrops jararacussu (jararacussu)
• Cellular location: Secreted : Q8AXY1
• Total number of polymer chains: 1
• Total formula weight: 13698.48

Authors

Murakami, M.T.,Cintra, A.C.,Gabdoulkhakov, A.,Genov, N.,Betzel, C.,Arni, R.K. (deposition date: 2005-05-05, release date: 2006-04-25, Last modification date: 2024-10-09)

Primary citation

Murakami, M.T.,Gabdoulkhakov, A.,Genov, N.,Cintra, A.C.,Betzel, C.,Arni, R.K.
Insights into metal ion binding in phospholipases A(2): ultra high-resolution crystal structures of an acidic phospholipase A(2) in the Ca(2+) free and bound states.
Biochimie, 88:543-549, 2006

PubMed Abstract: The electrophile Ca(2+) is an essential multifunctional co-factor in the phospholipase A(2) mediated hydrolysis of phospholipids. Crystal structures of an acidic phospholipase A(2) from the venom of Bothrops jararacussu have been determined both in the Ca(2+) free and bound states at 0.97 and 1.60 A resolutions, respectively. In the Ca(2+) bound state, the Ca(2+) ion is penta-coordinated by a distorted pyramidal cage of oxygen and nitrogen atoms that is significantly different to that observed in structures of other Group I/II phospholipases A(2). In the absence of Ca(2+), a water molecule occupies the position of the Ca(2+) ion and the side chain of Asp49 and the calcium-binding loop adopts a different conformation.

PubMed: 16376474
DOI: 10.1016/j.biochi.2005.10.014

Experimental method

X-RAY DIFFRACTION (0.97 Å)