1ayp: Difference between revisions
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[[Image:1ayp.gif|left|200px]] | [[Image:1ayp.gif|left|200px]] | ||
'''A PROBE MOLECULE COMPOSED OF SEVENTEEN PERCENT OF TOTAL DIFFRACTING MATTER GIVES CORRECT SOLUTIONS IN MOLECULAR REPLACEMENT''' | {{Structure | ||
|PDB= 1ayp |SIZE=350|CAPTION= <scene name='initialview01'>1ayp</scene>, resolution 2.57Å | |||
|SITE= | |||
|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> | |||
|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] | |||
|GENE= | |||
}} | |||
'''A PROBE MOLECULE COMPOSED OF SEVENTEEN PERCENT OF TOTAL DIFFRACTING MATTER GIVES CORRECT SOLUTIONS IN MOLECULAR REPLACEMENT''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1AYP is a [ | 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== | ||
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:// | 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]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''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
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| 1ayp, resolution 2.57Å | |||||||||||||
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| Ligands: | CA and INB | ||||||||||||
| 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
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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