3wpk

From Proteopedia
Jump to navigation Jump to search

SPATIOTEMPORAL DEVELOPMENT of SOAKED PROTEIN CRYSTAL; 750 SECSPATIOTEMPORAL DEVELOPMENT of SOAKED PROTEIN CRYSTAL; 750 SEC

Structural highlights

3wpk is a 1 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LYSC_CHICK Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus.[1]

Publication Abstract from PubMed

Crystal soaking is widely performed in biological crystallography. This paper reports time-resolved X-ray crystallographic and microtomographic analyses of tetragonal crystals of chicken egg-white lysozyme soaked in mother liquor containing potassium hexachloroplatinate. The microtomographic analysis showed that X-ray attenuation spread from the superficial layer of the crystal and then to the crystal core. The crystallographic analyses indicated that platinum sites can be classified into two groups from the temporal development of the electron densities. A soaking process consisting of binding-rate-driven and equilibrium-driven layers is proposed to describe these results. This study suggests that the composition of chemical and structural species resulting from the soaking process varies depending on the position in the crystal.

Spatiotemporal development of soaked protein crystal.,Mizutani R, Shimizu Y, Saiga R, Ueno G, Nakamura Y, Takeuchi A, Uesugi K, Suzuki Y Sci Rep. 2014 Jul 21;4:5731. doi: 10.1038/srep05731. PMID:25043871[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Maehashi K, Matano M, Irisawa T, Uchino M, Kashiwagi Y, Watanabe T. Molecular characterization of goose- and chicken-type lysozymes in emu (Dromaius novaehollandiae): evidence for extremely low lysozyme levels in emu egg white. Gene. 2012 Jan 15;492(1):244-9. doi: 10.1016/j.gene.2011.10.021. Epub 2011 Oct, 25. PMID:22044478 doi:10.1016/j.gene.2011.10.021
  2. Mizutani R, Shimizu Y, Saiga R, Ueno G, Nakamura Y, Takeuchi A, Uesugi K, Suzuki Y. Spatiotemporal development of soaked protein crystal. Sci Rep. 2014 Jul 21;4:5731. doi: 10.1038/srep05731. PMID:25043871 doi:http://dx.doi.org/10.1038/srep05731

3wpk, resolution 2.00Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA