1HSW

LYSOZYME (MUCOPEPTIDE N-ACETYLMURAMYL HYDROLASE)

Summary for 1HSW

• Entry DOI: 10.2210/pdb1hsw/pdb
• Descriptor: LYSOZYME (2 entities in total)
• Functional Keywords: hydrolase, glycosidase, enzyme-orthorhombic 88% r.h. form
• Biological source: Gallus gallus (chicken)
• Cellular location: Secreted: P00698
• Total number of polymer chains: 1
• Total formula weight: 14331.16

Authors

Sukumar, N.,Biswal, B.K.,Vijayan, M. (deposition date: 1998-06-04, release date: 1998-08-12, Last modification date: 2024-10-23)

Primary citation

Sukumar, N.,Biswal, B.K.,Vijayan, M.
Structures of orthorhombic lysozyme grown at basic pH and its low-humidity variant.
Acta Crystallogr.,Sect.D, 55:934-937, 1999

PubMed Abstract: The structures of orthorhombic lysozyme grown at basic pH and its low-humidity variant have been solved and refined at 1.9 and 2.0 A resolution, respectively. A comparison of the native structure with those of crystals grown at acidic pH does not show any systematic pH-dependent difference in the molecular geometry. The conformations, mutual orientation and interactions of the catalytic residues Glu35 and Asp52 also remain unchanged. However, comparison between the native and low-humidity forms in the orthorhombic form show that the changes in molecular geometry which accompany the water-mediated transformation to the low-humidity form are more pronounced in the C-terminal residues than in the other regions of the molecule. During the transformation from the native to the low-humidity form, the locations of only about half the water molecules in the hydration shell remain unchanged, but the hydration shell as a whole moves along with the protein molecule.

PubMed: 10089340
DOI: 10.1107/S0907444998015522

Experimental method

X-RAY DIFFRACTION (2 Å)