1RRL

Soybean Lipoxygenase (LOX-3) at 93K at 2.0 A resolution

Summary for 1RRL

• Entry DOI: 10.2210/pdb1rrl/pdb
• Related: 1IK3 1LNH 1NO3 1RRH
• Descriptor: Seed lipoxygenase-3, FE (II) ION (3 entities in total)
• Functional Keywords: oxidoreductase, iron metalloprotein, lipoxygenase
• Biological source: Glycine max (soybean)
• Cellular location: Cytoplasm: P09186
• Total number of polymer chains: 2
• Total formula weight: 193949.69

Authors

Borbulevych, O.Y.,Jankun, J.,Skrzypczak-Jankun, E. (deposition date: 2003-12-08, release date: 2004-12-21, Last modification date: 2023-08-23)

Primary citation

Skrzypczak-Jankun, E.,BORBULEVYCH, O.Y.,ZAVODSZKY, M.I.,BARANSKI, M.R.,PADMANABHAN, K.,PETRICEK, V.,JANKUN, J.
Effect of crystal freezing and small-molecule binding on internal cavity size in a large protein: X-ray and docking studies of lipoxygenase at ambient and low temperature at 2.0 A resolution.
Acta Crystallogr.,Sect.D, 62:766-775, 2006

PubMed Abstract: Flash-freezing is a technique that is commonly used nowadays to collect diffraction data for X-ray structural analysis. It can affect both the crystal and molecular structure and the molecule's surface, as well as the internal cavities. X-ray structural data often serve as a template for the protein receptor in docking calculations. Thus, the size and shape of the binding site determines which small molecules could be found as potential ligands in silico, especially during high-throughput rigid docking. Data were analyzed for wild soybean lipoxygenase-3 (MW 97 kDa) at 293 and 93 K and compared with the results from studies of its molecular complexes with known inhibitors, structures published by others for a derivative of the same enzyme (98 K) or a topologically close isozyme lipoxygenase-1 (at ambient temperature and 100 K). Analysis of these data allows the following conclusions. (i) Very small changes in the relative orientation of the molecules in the crystal can cause major changes in the crystal reciprocal lattice. (ii) The volume of the internal cavities can ;shrink' by several percent upon freezing even when the unit-cell and the protein molecular volume show changes of only 1-2%. (iii) Using a receptor structure determined based on cryogenic data as a target for computational screening requires flexible docking to enable the expansion of the binding-site cavity and sampling of the alternative conformations of the crucial residues.

PubMed: 16790932
DOI: 10.1107/S0907444906016982

Experimental method

X-RAY DIFFRACTION (2.09 Å)