1YTT

YB SUBSTITUTED SUBTILISIN FRAGMENT OF MANNOSE BINDING PROTEIN-A (SUB-MBP-A), MAD STRUCTURE AT 110K

Summary for 1YTT

• Entry DOI: 10.2210/pdb1ytt/pdb
• Descriptor: MANNOSE-BINDING PROTEIN A, YTTERBIUM (III) ION (3 entities in total)
• Functional Keywords: carbohydrate, recognition domain, calcium dependent, mannose-binding protein
• Biological source: Rattus norvegicus (Norway rat)
• Total number of polymer chains: 2
• Total formula weight: 26068.46

Authors

Burling, F.T.,Weis, W.I.,Flaherty, K.M.,Brunger, A.T. (deposition date: 1995-11-09, release date: 1996-06-10, Last modification date: 2024-10-23)

Primary citation

Burling, F.T.,Weis, W.I.,Flaherty, K.M.,Brunger, A.T.
Direct observation of protein solvation and discrete disorder with experimental crystallographic phases.
Science, 271:72-77, 1996

PubMed Abstract: A complete and accurate set of experimental crystallographic phases to a resolution of 1.8 angstroms was obtained for a 230-residue dimeric fragment of rat mannose-binding protein A with the use of multiwavelength anomalous dispersion (MAD) phasing. An accurate image of the crystal structure could thus be obtained without resort to phases calculated from a model. Partially reduced disulfide bonds, local disorder, and differences in the mobility of chemically equivalent molecules are apparent in the experimental electron density map. A solvation layer is visible that includes well-ordered sites of hydration around polar and charged protein atoms, as well as diffuse, partially disordered solvent shells around exposed hydrophobic groups. Because the experimental phases and the resulting electron density map are free from the influence of a model, they provide a stringent test of theoretical models of macromolecular solvation, motion, and conformational heterogeneity.

PubMed: 8539602

Experimental method

X-RAY DIFFRACTION (1.8 Å)