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


{{Structure
==THE ALPHA ANEURISM: A STRUCTURAL MOTIF REVEALED IN AN INSERTION MUTANT OF STAPHYLOCOCCAL NUCLEASE==
|PDB= 1sty |SIZE=350|CAPTION= <scene name='initialview01'>1sty</scene>, resolution 1.67&Aring;
<StructureSection load='1sty' size='340' side='right'caption='[[1sty]], [[Resolution|resolution]] 1.67&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=THP:THYMIDINE-3&#39;,5&#39;-DIPHOSPHATE'>THP</scene>
<table><tr><td colspan='2'>[[1sty]] 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=1STY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1STY FirstGlance]. <br>
|ACTIVITY= [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]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.67&#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>
}}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1sty FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sty OCA], [https://pdbe.org/1sty PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sty RCSB], [https://www.ebi.ac.uk/pdbsum/1sty PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sty ProSAT]</span></td></tr>
</table>
== 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/st/1sty_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=1sty ConSurf].
<div style="clear:both"></div>


'''THE ALPHA ANEURISM: A STRUCTURAL MOTIF REVEALED IN AN INSERTION MUTANT OF STAPHYLOCOCCAL NUCLEASE'''
==See Also==
 
*[[Staphylococcal nuclease 3D structures|Staphylococcal nuclease 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
The x-ray crystal structure of a mutant of staphylococcal nuclease that contains a single glycine residue inserted in the C-terminal alpha-helix has been solved to 1.67 A resolution and refined to a crystallographic R value of 0.170. This inserted glycine residue is accommodated in the alpha-helix by formation of a previously uncharacterized bulge, which we term the alpha aneurism. A conformational search of known protein structures has identified the alpha aneurism in a number of protein families, including the histocompatibility antigens and hemoglobins.
[[Category: Large Structures]]
 
==About this Structure==
1STY 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=1STY OCA].
 
==Reference==
The alpha aneurism: a structural motif revealed in an insertion mutant of staphylococcal nuclease., Keefe LJ, Sondek J, Shortle D, Lattman EE, Proc Natl Acad Sci U S A. 1993 Apr 15;90(8):3275-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8475069 8475069]
[[Category: Micrococcal nuclease]]
[[Category: Single protein]]
[[Category: Staphylococcus aureus]]
[[Category: Staphylococcus aureus]]
[[Category: Keefe, L J.]]
[[Category: Keefe LJ]]
[[Category: Lattman, E E.]]
[[Category: Lattman EE]]
[[Category: CA]]
[[Category: THP]]
[[Category: hydrolase (phosphoric diester)]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 13:39:15 2008''

Latest revision as of 11:33, 14 February 2024

THE ALPHA ANEURISM: A STRUCTURAL MOTIF REVEALED IN AN INSERTION MUTANT OF STAPHYLOCOCCAL NUCLEASETHE ALPHA ANEURISM: A STRUCTURAL MOTIF REVEALED IN AN INSERTION MUTANT OF STAPHYLOCOCCAL NUCLEASE

Structural highlights

1sty is a 1 chain structure with sequence from Staphylococcus aureus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.67Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

NUC_STAAU Enzyme that catalyzes the hydrolysis of both DNA and RNA at the 5' position of the phosphodiester bond.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1sty, resolution 1.67Å

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