1ytt: Difference between revisions

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[[Image:1ytt.jpg|left|200px]]
[[Image:1ytt.jpg|left|200px]]


{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ytt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ytt OCA], [http://www.ebi.ac.uk/pdbsum/1ytt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ytt RCSB]</span>
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'''YB SUBSTITUTED SUBTILISIN FRAGMENT OF MANNOSE BINDING PROTEIN-A (SUB-MBP-A), MAD STRUCTURE AT 110K'''
'''YB SUBSTITUTED SUBTILISIN FRAGMENT OF MANNOSE BINDING PROTEIN-A (SUB-MBP-A), MAD STRUCTURE AT 110K'''
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[[Category: Flaherty, K M.]]
[[Category: Flaherty, K M.]]
[[Category: Weis, W I.]]
[[Category: Weis, W I.]]
[[Category: calcium dependent]]
[[Category: Calcium dependent]]
[[Category: carbohydrate]]
[[Category: Carbohydrate]]
[[Category: mannose-binding protein]]
[[Category: Mannose-binding protein]]
[[Category: recognition domain]]
[[Category: Recognition domain]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 16:46:52 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:22:25 2008''

Revision as of 16:46, 3 May 2008

File:1ytt.jpg

Template:STRUCTURE 1ytt

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


OverviewOverview

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.

About this StructureAbout this Structure

1YTT is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

ReferenceReference

Direct observation of protein solvation and discrete disorder with experimental crystallographic phases., Burling FT, Weis WI, Flaherty KM, Brunger AT, Science. 1996 Jan 5;271(5245):72-7. PMID:8539602 Page seeded by OCA on Sat May 3 16:46:52 2008

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