1ytt: Difference between revisions

Revision as of 12:16, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1ytt.png

Template:STRUCTURE 1ytt

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

Template:ABSTRACT PUBMED 8539602

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 Sun Jul 27 12:16:39 2008

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OCA

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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===
-==Overview==
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-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_8539602}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8539602 is the PubMed ID number.
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 ==About this Structure==
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 [[Category: Mannose-binding protein]]
 [[Category: Recognition domain]]
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