1syb: Difference between revisions

Revision as of 09:16, 3 May 2008

TRANSFER OF A BETA-TURN STRUCTURE TO A NEW PROTEIN CONTEXT

OverviewOverview

Four-residue beta-turns and larger loop structures represent a significant fraction of globular protein surfaces and play an important role in determining the conformation and specificity of enzyme active sites and antibody-combining sites. Turns are an attractive starting point to develop protein design methods, as they involve a small number of consecutive residues, adopt a limited number of defined conformations and are minimally constrained by packing interactions with the remainder of the protein. The ability to substitute one beta-turn geometry for another will extend protein engineering beyond the redecoration of fixed backbone conformations to include local restructuring and the repositioning of surface side chains. To determine the feasibility and to examine the effect of such a structural modification on the fold and thermodynamic stability of a globular protein, we have substituted a five-residue turn sequence from concanavalin A for a type I' beta-turn in staphylococcal nuclease. The resulting hybrid protein is folded and has full nuclease enzymatic activity but reduced thermodynamic stability. The crystal structure of the hybrid protein reveals that the guest turn sequence retains the conformation of the parent concanavalin A structure when substituted in the nuclease host.

About this StructureAbout this Structure

1SYB is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.

ReferenceReference

Transfer of a beta-turn structure to a new protein context., Hynes TR, Kautz RA, Goodman MA, Gill JF, Fox RO, Nature. 1989 May 4;339(6219):73-6. PMID:2716830 Page seeded by OCA on Sat May 3 09:16:31 2008

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OCA

@@ Line 1: / Line 1: @@
 [[Image:1syb.jpg|left|200px]]
- {{Structure
+<!--
-|PDB= 1syb |SIZE=350|CAPTION= <scene name='initialview01'>1syb</scene>, resolution 1.8&Aring;
+The line below this paragraph, containing "STRUCTURE_1syb", creates the "Structure Box" on the page.
-|SITE=
+You may change the PDB parameter (which sets the PDB file loaded into the applet)
-|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=THP:THYMIDINE-3&#39;,5&#39;-DIPHOSPHATE'>THP</scene>
+or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Micrococcal_nuclease Micrococcal nuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.31.1 3.1.31.1] </span>
+or leave the SCENE parameter empty for the default display.
-|GENE=
+-->
-|DOMAIN=
+{{STRUCTURE_1syb|  PDB=1syb  |  SCENE=  }}
-|RELATEDENTRY=
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1syb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1syb OCA], [http://www.ebi.ac.uk/pdbsum/1syb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1syb RCSB]</span>
-}}
 '''TRANSFER OF A BETA-TURN STRUCTURE TO A NEW PROTEIN CONTEXT'''
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 [[Category: Hynes, T R.]]
 [[Category: Kautz, R A.]]
-[[Category: hydrolase(phosphoric diester)]]
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 09:16:31 2008''
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:48:39 2008''