1FB2

STRUCTURE OF PHOSPHOLIPASE A2 FROM DABOIA RUSSELLI PULCHELLA AT 1.95

Summary for 1FB2

• Entry DOI: 10.2210/pdb1fb2/pdb
• Related: 1cl5
• Descriptor: PHOSPHOLIPASE A2 (2 entities in total)
• Functional Keywords: phospholipase a2, daboia russelli pulchella, neurotoxic, toxin
• Biological source: Daboia russellii pulchella
• Cellular location: Secreted : P59071
• Total number of polymer chains: 2
• Total formula weight: 27259.53

Authors

Chandra, V.,Kaur, P.,Betzel, C.,Singh, T.P. (deposition date: 2000-07-14, release date: 2001-07-25, Last modification date: 2024-11-06)

Primary citation

Chandra, V.,Kaur, P.,Jasti, J.,Betzel, C.,Singh, T.P.
Regulation of catalytic function by molecular association: structure of phospholipase A2 from Daboia russelli pulchella (DPLA2) at 1.9 A resolution.
Acta Crystallogr.,Sect.D, 57:1793-1798, 2001

PubMed Abstract: The crystal structure of phospholipase A(2) from the venom of Daboia russelli pulchella has been refined to an R factor of 0.216 using 17,922 reflections to 1.9 A resolution. The structure contains two crystallographically independent molecules in the asymmetric unit. The overall conformations of the two molecules are essentially the same except for three regions, namely the calcium-binding loop including Trp31, the beta-wing and the C-terminal residues 119-131. Although these differences have apparently been caused by molecular packing, they seem to have functional relevance. Particularly noteworthy is the conformation of Trp31, which is favourable for substrate binding in one molecule as it is aligned with one of the side walls of the hydrophobic channel, whereas in the other molecule it is located at the mouth of the channel, thereby blocking the entry of substrates leading to loss of activity. This feature is unique to the present structure and does not occur in the dimers and trimers of other PLA(2)s.

PubMed: 11717491
DOI: 10.1107/S0907444901014524

Experimental method

X-RAY DIFFRACTION (1.95 Å)