1sta: Difference between revisions

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[[Image:1sta.jpg|left|200px]]<br /><applet load="1sta" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1sta.jpg|left|200px]]
caption="1sta, resolution 1.70&Aring;" />
 
'''ACCOMMODATION OF INSERTION MUTATIONS ON THE SURFACE AND IN THE INTERIOR OF STAPHYLOCOCCAL NUCLEASE'''<br />
{{Structure
|PDB= 1sta |SIZE=350|CAPTION= <scene name='initialview01'>1sta</scene>, resolution 1.70&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=THP:THYMIDINE-3',5'-DIPHOSPHATE'>THP</scene>
|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]
|GENE=
}}
 
'''ACCOMMODATION OF INSERTION MUTATIONS ON THE SURFACE AND IN THE INTERIOR OF STAPHYLOCOCCAL NUCLEASE'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1STA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=THP:'>THP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1STA OCA].  
1STA 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=1STA OCA].  


==Reference==
==Reference==
Accommodation of insertion mutations on the surface and in the interior of staphylococcal nuclease., Keefe LJ, Quirk S, Gittis A, Sondek J, Lattman EE, Protein Sci. 1994 Mar;3(3):391-401. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8019410 8019410]
Accommodation of insertion mutations on the surface and in the interior of staphylococcal nuclease., Keefe LJ, Quirk S, Gittis A, Sondek J, Lattman EE, Protein Sci. 1994 Mar;3(3):391-401. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8019410 8019410]
[[Category: Micrococcal nuclease]]
[[Category: Micrococcal nuclease]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: hydrolase(phosphoric diester)]]
[[Category: hydrolase(phosphoric diester)]]


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Revision as of 15:09, 20 March 2008

File:1sta.jpg


PDB ID 1sta

Drag the structure with the mouse to rotate
, resolution 1.70Å
Ligands: and
Activity: Micrococcal nuclease, with EC number 3.1.31.1
Coordinates: save as pdb, mmCIF, xml



ACCOMMODATION OF INSERTION MUTATIONS ON THE SURFACE AND IN THE INTERIOR OF STAPHYLOCOCCAL NUCLEASE


OverviewOverview

Alignment of homologous amino acid sequences reveals that insertion mutations are fairly common in evolution. Hitherto, the structural consequences of insertion mutations on the surface and in the interior of proteins of known structures have received little attention. We report here the high-resolution X-ray crystal structures of 2 site-directed insertion mutants of staphylococcal nuclease. The structure of the first insertion mutant, in which 2 glycine residues were inserted on the protein surface in the amino-terminal beta-strand, has been solved to 1.70 A resolution and refined to a crystallographic R value of 0.182. The inserted residues are accommodated in a special 3-residue beta-bulge. A bridging water molecule in the newly created cavity satisfies the hydrogen bonding requirements of the beta-sheet by forming a bifurcated hydrogen bond to 1 beta-strand, and a single hydrogen bond to the other beta-strand. The second insertion mutant contains a single leucine residue inserted at the end of the third beta-strand. The structure was solved to 2.0 A resolution and refined to a final R value of 0.196. The insertion is accommodated in a register shift that changes the conformation of the flexible loop portion of the molecule, relaxing and widening the omega turn. This structural alteration results in changes in position and coordination of a bound calcium ion important for catalysis. These structures illustrate important differences in how amino acid insertions are accommodated: as localized bulges, and as extensive register shifts.

About this StructureAbout this Structure

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

ReferenceReference

Accommodation of insertion mutations on the surface and in the interior of staphylococcal nuclease., Keefe LJ, Quirk S, Gittis A, Sondek J, Lattman EE, Protein Sci. 1994 Mar;3(3):391-401. PMID:8019410

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