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


{{Structure
==TRANSFER OF A BETA-TURN STRUCTURE TO A NEW PROTEIN CONTEXT==
|PDB= 1syb |SIZE=350|CAPTION= <scene name='initialview01'>1syb</scene>, resolution 1.8&Aring;
<StructureSection load='1syb' size='340' side='right'caption='[[1syb]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=THP:THYMIDINE-3&#39;,5&#39;-DIPHOSPHATE'>THP</scene>
<table><tr><td colspan='2'>[[1syb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SYB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SYB FirstGlance]. <br>
|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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
|GENE=
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=THP:THYMIDINE-3,5-DIPHOSPHATE'>THP</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1syb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1syb OCA], [https://pdbe.org/1syb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1syb RCSB], [https://www.ebi.ac.uk/pdbsum/1syb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1syb ProSAT]</span></td></tr>
|RELATEDENTRY=
</table>
|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>
== Function ==
}}
[https://www.uniprot.org/uniprot/NUC_STAAU NUC_STAAU] Enzyme that catalyzes the hydrolysis of both DNA and RNA at the 5' position of the phosphodiester bond.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sy/1syb_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1syb ConSurf].
<div style="clear:both"></div>


'''TRANSFER OF A BETA-TURN STRUCTURE TO A NEW PROTEIN CONTEXT'''
==See Also==
 
*[[Staphylococcal nuclease 3D structures|Staphylococcal nuclease 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
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.
[[Category: Large Structures]]
 
==About this Structure==
1SYB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SYB OCA].
 
==Reference==
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:[http://www.ncbi.nlm.nih.gov/pubmed/2716830 2716830]
[[Category: Micrococcal nuclease]]
[[Category: Single protein]]
[[Category: Staphylococcus aureus]]
[[Category: Staphylococcus aureus]]
[[Category: Fox, R O.]]
[[Category: Fox RO]]
[[Category: Gill, J F.]]
[[Category: Gill JF]]
[[Category: Goodman, M A.]]
[[Category: Goodman MA]]
[[Category: Hynes, T R.]]
[[Category: Hynes TR]]
[[Category: Kautz, R A.]]
[[Category: Kautz RA]]
[[Category: hydrolase(phosphoric diester)]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:48:39 2008''

Latest revision as of 08:34, 14 February 2024

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

1syb, resolution 1.80Å

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