1ytt
From Proteopedia
(New page: 200px<br /><applet load="1ytt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ytt, resolution 1.8Å" /> '''YB SUBSTITUTED SUBTIL...) |
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| - | [[Image:1ytt.jpg|left|200px]]<br /><applet load="1ytt" size=" | + | [[Image:1ytt.jpg|left|200px]]<br /><applet load="1ytt" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ytt, resolution 1.8Å" /> | caption="1ytt, resolution 1.8Å" /> | ||
'''YB SUBSTITUTED SUBTILISIN FRAGMENT OF MANNOSE BINDING PROTEIN-A (SUB-MBP-A), MAD STRUCTURE AT 110K'''<br /> | '''YB SUBSTITUTED SUBTILISIN FRAGMENT OF MANNOSE BINDING PROTEIN-A (SUB-MBP-A), MAD STRUCTURE AT 110K'''<br /> | ||
==Overview== | ==Overview== | ||
| - | A complete and accurate set of experimental crystallographic phases to a | + | 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 Structure== | ==About this Structure== | ||
| - | 1YTT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with YB as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1YTT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=YB:'>YB</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YTT OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Brunger, A | + | [[Category: Brunger, A T.]] |
| - | [[Category: Burling, F | + | [[Category: Burling, F T.]] |
| - | [[Category: Flaherty, K | + | [[Category: Flaherty, K M.]] |
| - | [[Category: Weis, W | + | [[Category: Weis, W I.]] |
[[Category: YB]] | [[Category: YB]] | ||
[[Category: calcium dependent]] | [[Category: calcium dependent]] | ||
| Line 23: | Line 23: | ||
[[Category: recognition domain]] | [[Category: recognition domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:09:03 2008'' |
Revision as of 14:09, 21 February 2008
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YB SUBSTITUTED SUBTILISIN FRAGMENT OF MANNOSE BINDING PROTEIN-A (SUB-MBP-A), MAD STRUCTURE AT 110K
Overview
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 Structure
1YTT is a Single protein structure of sequence from Rattus norvegicus with as ligand. Full crystallographic information is available from OCA.
Reference
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 Thu Feb 21 16:09:03 2008
