1ayp

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[[Image:1ayp.gif|left|200px]]<br /><applet load="1ayp" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ayp.gif|left|200px]]
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caption="1ayp, resolution 2.57&Aring;" />
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'''A PROBE MOLECULE COMPOSED OF SEVENTEEN PERCENT OF TOTAL DIFFRACTING MATTER GIVES CORRECT SOLUTIONS IN MOLECULAR REPLACEMENT'''<br />
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{{Structure
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|PDB= 1ayp |SIZE=350|CAPTION= <scene name='initialview01'>1ayp</scene>, resolution 2.57&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=INB:1-OCTADECYL-2-ACETAMIDO-2-DEOXY-SN-GLYCEROL-3-PHOSPHOETHYLMETHYL SULFIDE'>INB</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Phospholipase_A(2) Phospholipase A(2)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.4 3.1.1.4]
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|GENE=
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}}
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'''A PROBE MOLECULE COMPOSED OF SEVENTEEN PERCENT OF TOTAL DIFFRACTING MATTER GIVES CORRECT SOLUTIONS IN MOLECULAR REPLACEMENT'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1AYP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=INB:'>INB</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phospholipase_A(2) Phospholipase A(2)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.4 3.1.1.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AYP OCA].
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1AYP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AYP OCA].
==Reference==
==Reference==
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A probe molecule composed of seventeen percent of total diffracting matter gives correct solutions in molecular replacement., Oh BH, Acta Crystallogr D Biol Crystallogr. 1995 Mar 1;51(Pt 2):140-4. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15299314 15299314]
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A probe molecule composed of seventeen percent of total diffracting matter gives correct solutions in molecular replacement., Oh BH, Acta Crystallogr D Biol Crystallogr. 1995 Mar 1;51(Pt 2):140-4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15299314 15299314]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Phospholipase A(2)]]
[[Category: Phospholipase A(2)]]
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[[Category: hydrolase]]
[[Category: hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:49:43 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:04:05 2008''

Revision as of 08:04, 20 March 2008

Image:1ayp.gif


PDB ID 1ayp

Drag the structure with the mouse to rotate
, resolution 2.57Å
Ligands: and
Activity: Phospholipase A(2), with EC number 3.1.1.4
Coordinates: save as pdb, mmCIF, xml



A PROBE MOLECULE COMPOSED OF SEVENTEEN PERCENT OF TOTAL DIFFRACTING MATTER GIVES CORRECT SOLUTIONS IN MOLECULAR REPLACEMENT


Contents

Overview

It is often found in the crystallization of enzyme-inhibitor complexes that an inhibitor causes crystal packing which is different to that of native protein. This is the case for crystals of human non-pancreatic secreted phospholipase A(2) (124 residues) containing six molecules in the asymmetric unit when the protein is complexed with a potential acylamino analogue of a phospholid. The hexameric structure was determined by molecular replacement using the structure of monomeric native protein as a probe. As an extension to the experiment, it was tested whether a backbone polypeptide composed of 17% of a known monomeric structure could find its correct position on a target molecule in molecular replacement. A probe model composed of the backbone atoms of the N-terminal 77 residues of lysine-, arginine-, ornithine-binding protein (LAO, a total of 238 residues) liganded with lysine correctly finds its position on LAO liganded with histidine which crystallizes as a monomer in the asymmetric unit. The results indicate that as little as 17% of total diffracting matter can be used in molecular replacement to solve crystal structures or to obtain phase information which can be combined with phases obtained by the isomorphous-replacement method.

Disease

Known diseases associated with this structure: Colorectal cancer, sporadic OMIM:[172411]

About this Structure

1AYP is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

A probe molecule composed of seventeen percent of total diffracting matter gives correct solutions in molecular replacement., Oh BH, Acta Crystallogr D Biol Crystallogr. 1995 Mar 1;51(Pt 2):140-4. PMID:15299314

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