1ops: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 7: Line 7:
|ACTIVITY=  
|ACTIVITY=  
|GENE=  
|GENE=  
|DOMAIN=
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ops FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ops OCA], [http://www.ebi.ac.uk/pdbsum/1ops PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ops RCSB]</span>
}}
}}


Line 34: Line 37:
[[Category: pretzel fold]]
[[Category: pretzel fold]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:14:01 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:48:43 2008''

Revision as of 22:48, 30 March 2008

File:1ops.jpg


PDB ID 1ops

Drag the structure with the mouse to rotate
, resolution 2.00Å
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



ICE-BINDING SURFACE ON A TYPE III ANTIFREEZE PROTEIN FROM OCEAN POUT


OverviewOverview

Antifreeze proteins (AFPs) adsorb to surfaces of growing ice crystals, thereby arresting their growth. The prevailing hypothesis explains the nature of adsorption in terms of a match between the hydrophilic side chains on the AFP's ice-binding surface (IBS) and the water molecules on the ice surface. The number and spatial arrangement of hydrogen bonds thus formed have been proposed to account, respectively, for the binding affinity and specificity. The crystal structure of a type III AFP from ocean pout (isoform HPLC-3) has been determined to 2.0-A resolution. The structure reveals an internal dyad motif formed by two 19-residue, loop-shaped elements. Based on of the flatness observed on the type I alpha-helical AFP's IBS, an automated algorithm was developed to analyze the surface planarity of the globular type III AFP and was used to identify the IBS on this protein. The surface with the highest flatness score is formed by one loop of the dyad motif and is identical to the IBS deduced from earlier mutagenesis studies. Interestingly, 67% of this surface contains nonpolar solvent-accessible surface area. The success of our approach to identifying the IBS on an AFP, without considering the presence of polar side chains, indicates that flatness is the first approximation of an IBS. We further propose that the specificity of interactions between an IBS and a particular ice-crystallographic plane arises from surface complementarity.

About this StructureAbout this Structure

1OPS is a Single protein structure of sequence from Macrozoarces americanus. Full crystallographic information is available from OCA.

ReferenceReference

Identification of the ice-binding surface on a type III antifreeze protein with a "flatness function" algorithm., Yang DS, Hon WC, Bubanko S, Xue Y, Seetharaman J, Hew CL, Sicheri F, Biophys J. 1998 May;74(5):2142-51. PMID:9591641

Page seeded by OCA on Sun Mar 30 22:48:43 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA